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Molecular Imprinting of Complex Matrices at Localized Surface Plasmon Resonance Biosensors for Screening of Global Interactions of Polyphenols and Proteins

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† BioMark Sensor Research-CINTESIS, Instituto Superior de Engenharia do Porto, Porto 4200-072, Portugal

‡ REQUIMTE/LAQV, Departamento de Química e Bioquímica, Faculdade de Ciências da Universidade do Porto, Porto 4169-007, Portugal

§ Interdisciplinary Nanoscience Center (iNANO), Aarhus University, Aarhus 8000, Denmark

∥ Department of Chemistry, Lomonosov Moscow State University, Moscow 119991, Russia

⊥ Department of Molecular Biology and Genetics, Aarhus University, Aarhus 8000, Denmark

*E-mail: [email protected].

Cite this: ACS Sens. 2016, 1, 3, 258-264

Publication Date (Web):December 25, 2015

https://doi.org/10.1021/acssensors.5b00054

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Abstract

Molecular imprinting polymers (MIP) have been applied to capture and stabilize complex protein matrices at plasmonic sensor surfaces. Ultrathin MIP layers at the surface of gold nanodisks enable the label free quantification of global interactions of polyphenols with protein mixtures. Separate polyphenols (catechin, procyanidin B3- catechin dimer, and PGG-pentagalloyl glucose) give specific and different binding levels to the MIP supported saliva plasmonic sensor. The demonstrated biosensor has application to study bioavailability of polyphenols or evaluation of local retention of small drug molecules.

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Polyphenols, present in dietary fruit and vegetables, are proposed to aid in prevention of a broad range of diseases such as Alzheimer’s,(1-3) Parkinson’s,(1) coronary heart diseases,(4-6) and cancer,(7-9) as well as provide antibacterial,(10, 11) antiviral,(10) anticarcinogenic,(12-14) and anti-inflammatory(15-17) activities. The specific roles of polyphenols in biological processes are not fully understood but have been highlighted as a group of promising therapeutic or protective agents regarding their ability to bind to proteins or block active sites.(8, 18-22) Polyphenols, in common with many small drug molecules, exhibit a broad and varied association with proteins and other biomolecules, which has strong impact on their bioavailability. The first barrier to bioavailability is inside the mouth, where polyphenols interact with salivary proteins, such as amylase (AMY), mucins, and proline-rich proteins (PRP) altering the composition and concentrations available for uptake in the digestive tract. Polyphenols reaching their site of action, either via digestion or therapeutic delivery, will bind to the complex protein environment giving a complex set of global interactions likely determining their effect. Currently, there is a lack of effective tools to study and characterize the specific and global interactions between small molecules, such as polyphenols and complex protein matrices.

Localized surface plasmon resonances (LSPR) have been applied to give high sensitivity label-free optical detection and quantification.(23) Moreover, LSPR approaches have more localized volumes of detection than conventional surface plasmon resonance techniques, allowing higher sensitivity for thin sensor films and less influence of bulk changes in refractive index. Biomolecular recognition elements (typically antibodies(24)) immobilized at the surface of a metal nanostructure act to concentrate the analyte within the local optical field of the plasmonic resonance. Other specific molecular interactions have been applied including DNA–DNA,(25) aptamer–protein,(26, 27) protein–protein,(28, 29) enzyme–substrate,(30) and protein–small compound.(31, 32)

Molecular imprinted polymers (MIP) are an attractive alternative to antibodies(33) due to their inherent stability and short time preparation. The cross-linking of functional monomers around a target molecule enables the formation of specific recognition sites, which allows the targeting of a specific protein by a complex polymer surface. The recognition sites are shaped and sized according to the template/target protein positioning and orientation, resulting from the self-assembling mechanism of functional monomer units. As a result molecular imprinting gives both the ability for each cavity to selectively recognize and stabilize a target molecule from a complex matrix as well as to make sensor surfaces reusable. For LSPR sensors, MIP can provide a thin sensing layer, targeting the high sensitivity/high optical field regions around the nanosensor which has been recently demonstrated.(34) To date, MIP layers have been used to recognize single specific analytes from a mixture.

Here, we report for the first time the molecular imprinting and stabilization of a complex protein matrix. We demonstrate a novel application of molecular imprinting and plasmonics to capture a matrix of human saliva proteins close to the surface of an LSPR sensor. The reusable plasmonic sensor combined molecular imprinting to capture a representative set of a complex protein matrix instead of the traditional application to selective capture a single analyte from a complex matrix.

Here, a natural complex matrix of salivary proteins was immobilized to simulate the oral cavity environment. We applied the complex sensor to follow the interactions of specific polyphenols (pentagalloyl glucose (PGG), procyanidin B3, and (+)-catechin) with human saliva, giving insight into the molecular diversity of polyphenol retention and activity in the oral cavity. The developed concept can be applied to bioavailability studies of polyphenols and other small molecules in a range of protein matrices and give information about tissue specific polyphenol binding affinity and local retention.

Experimental Section

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Au Nanodisks Fabrication

The Au nanodisks array was prepared based on our previous work.(32)

Molecular Imprinted Films

The imprinting process of both single (amylase) and multiple proteins matrix (saliva) started by creating anchor spots to link the imprinting polymer to the Au nanodisks surface. For that, the Au nanodisk substrates were first incubated overnight in 1 mL of thiophenecarboxylic acid 5 mM prepared in 10% ethanol. The proteins matrix (50 μL of AMY 10 μM or pure saliva) was physically adsorbed by incubating for 2 h at 4 °C followed by MQ water rinsing. The functional monomers (methacrylic acid and (vinylbenzyl)trimethylammonium chloride, 5 mM) were then added for 30 min each followed by overnight (12 h) polymerization by 1 mL of polymerization mixture containing ethylene glycol dimethacrylate, methyl acrylate, and ammonium persulfate 5 mM at 39 °C. After polymerization, the template removal was carried out by adding 50 μL of Proteinase K 500 μg/mL for 2 h at 37 °C. Nonimprinted materials were produced in parallel in the same way, but without the protein step.

LSPR Interaction Studies in a Flow System

Prior to interaction studies with polyphenol (catechin, PGG and B3), the rebinding step was performed by adding 100 μL of pure saliva and AMY to the imprinted surfaces. The polyphenol interacted individually with AMY or saliva, by injecting several standard solutions of increasing concentrations; for PGG, concentrations ranged from 0.1 to 955 μM; for catechin, concentrations ranged from 160 to 56 500 μM, and B3 100–57 000 μM at a flow rate of 50 μL/min. The spectra were collected by measuring the incident light that passes through the flow cell composed by the Au nanodisks substrates. The polyphenol and protein interacted for 2.5 min followed by 2.5 min of rinsing with buffer before spectra collection.

The overall modification steps were performed in steady state conditions, whereas their evaluation was in continuous flow mode.

Results and Discussion

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Molecular Imprinting Procedure on Au Nanodisks

Both saliva and α-amylase (AMY) were surface imprinted at LSPR sensor surfaces. Gold nanodisk LSPR sensors were fabricated on glass substrate by hole mask colloidal lithography.(35) The process (shown in Figure 1) used a 100 nm diameter colloidal template adsorbed on 200 nm polymer films followed by deposition of a 20 nm Titanium film evaporated by physical vapor deposition (PVD) to generate the hole-mask. Subsequently, 2 nm Ti and 20 nm Au were evaporated by PVD followed by mask lift-off to create Au disks. Full details are found in the Supporting Information.

Surface imprinting(36, 37) was applied to proteins preadsorbed at the nanodisks surfaces. Briefly, the imprinting process consisted of three main steps. First, a thiol layer was introduced overnight on the Au disks substrates playing an anchoring role between the disks and the imprinting material. The following step involved the physical adsorption of dense AMY or saliva layer (characterized by SDS PAGE, Supporting Information) on Au nanodisks for 2 h. Characterization of the preadsorbed protein layer was carried out by both surface plasmon resonance (SPR) and LSPR measurements combined with the known AMY crystal structure and using a random sequential adsorption model(38) (see Supporting Information Table S-2). The adsorbed AMY formed a thin, dense monolayer, whereas the complex protein layer forming from saliva formed a substantially thicker layer. Protein imprinting is a complex process that can be complicated by proteins’ conformational change; therefore, we used water-soluble monomers, cross-linkers, and initiators under mild conditions. Molecular imprinting binding sites formation included both negatively and positively charged monomers. The negative and positive monomers were added to the surface with adsorbed protein (AMY or Saliva) for 30 min each, and washed with Milli-Q water, followed by an overnight polymerization in the presence of neutral monomer/cross-linker and an initiator solution at 39 °C. The nature and outer surface structure of the proteins determined the localization of several charged groups over its entire surface. Therefore, before polymerization, charged monomers were allowed to establish noncovalent ionic interactions with the numerous protein charged spots (template) of opposite charge. The in situ polymerization process generated a network interlinking the charged monomers and the surface. The formed molecular imprint films were thinner than the expected sizes of the proteins which suggest that only the lower part of the protein was imprinted under the used conditions. In contrast to the binding sites, the surroundings are composed of neutral monomer which reduces nonspecific binding.(39) Finally, the third stage was the template removal, carried out at 39 °C by proteinase K, an efficient enzyme for protein digestion. The imprinting process allowed the production of two distinct smart materials: the AMY imprinted material (AIM) and the saliva imprinted material (SIM) on Au nanodisks. These smart materials were then used for template (AMY or saliva) rebinding followed by polyphenol interaction. As control, a nonimprinted polymer material (NIP) without protein adsorption was also produced on Au nanodisk substrates. The imprinting process details are described and confirmed by an electrochemical technique in the Supporting Information. The imprinting process was followed by characterization of the LSPR, by optical extinction spectroscopy (Shimadzu 3600 UV-vis-NIR).

The fabrication process brings in a small but significant sample to sample variation in the position and amplitude of the resonant optical extinction maxima, giving initial peak positions of 685 ± 11 nm in phosphate buffered saline (PBS), pH 7. This variation in the initial peak position has a negligible effect on the refractive index sensitivity allowing direct comparison of refractive index induced peak shifts. The imprinting process was followed by LSPR detection in a continuous flow system. Extinction spectra were collected while PBS running buffer was flowing through the chamber. The modifications steps measured by LSPR can be seen in Figure 2.

The physical adsorption of AMY and saliva on Au nanodisks induced an average peak shift of 1.94 ± 0.29 and 4.64 ± 1.04 nm, respectively, resulting from the increased refractive index close to the metal surface giving rise to a red shift of the plasmon peak. The formation of the polymer imprinting layers (combined with any associated removal of bound protein) resulted in an overall increased local refractive index of the Au nanodisks. This resulted in an additional red shift of 0.50 ± 0.01 and 1.18 ± 0.32 nm for AIM and SIM, respectively, while the peak shift of the control NIP was 1.60 ± 0.69 nm. Proteinase K was selected as the template removal agent, leading to a blue shift of 1.10 ± 0.31 and 1.81 ± 0.58 nm for AIM and SIM (corresponding to a reduction of refractive index close to the Au nanodisks), respectively, and a red shift of 0.38 ± 0.25 nm for NIP. These results suggest that protein fragments were removed from the binding sites at the MIP surfaces, while for the NIP the small red shift observed may be due to weakly adsorbed proteinase K molecules. All the details regarding the modification process and LSPR measurements are present in Supporting Information Figure S-3. The imprinting process was confirmed by a parallel electrochemical study using flat gold electrodes, as can be seen in Figures S-4 and 5 and Tables S-3 and 4 in the Supporting Information.

The decay length of the field enhancement around the Au nanodisks surface was previously estimated by FDTD simulations to be 17.7 ± 0.7 nm.(32, 40) It is known that the sensitivity decreases dramatically with the increasing distance from the surface. The polymer thickness with imprinted saliva was evaluated by atomic force microscopy (AFM) imaging showing a thin molecular imprinted polymer thickness of ∼4 nm on top of the Au nanodisks and ∼0.5 nm on the glass substrate between the disks (Figure S-6 in the Supporting Information). The imprinted and nonimprinted AMY polymer substrates were also measured by AFM in liquid shown in Figure 3, and details are found in the Supporting Information.

The presence of the template AMY led to a clearly altered topography at the sensor surface compared to the nonimprinted surface indicating that the imprinting process occurred at the nanodisk surface.

Rebinding Capability

Protein entrapment can be an issue for protein rebinding due to possible steric hindrance limitations; thus it is essential to promote a good protein removal. The use of thin polymers might be advantageous to facilitate protein removal. Both smart surfaces AIM and SIM were tested to evaluate rebinding capability. The results obtained for AMY rebinding on AIM and saliva rebinding on SIM (2 h) provided an LSPR red shift of 0.99 ± 0.35 and 1.79 ± 0.28 nm, respectively, correlating very well with the blue shift promoted by template removal, indicating a good rebinding capability. The protein removal from the multiple used smart materials provided an LSPR blue shift consistent with the previous results, 0.94 ± 0.40 nm for AMY and 1.71 ± 0.58 nm for saliva, showing the reusability of MIP samples (Table S-5 in the Supporting Information). Both saliva and AMY were also incubated on the NIP surface, promoting an additional peak shift of 1.21 ± 0.28 and 0.57 ± 0.21 nm, respectively. These results indicate that as expected both AMY and saliva can bind nonspecifically to surfaces with the AMY binding being comparable to that of the AMY MIP. The saliva imprinted surface provides more robust and higher specific responses. The capture of target proteins from saliva as achieved through the molecular imprinting of Au disks, with the salivary proteins being immobilized and available for use as a sensor element.

FDTD Calculations

Finite-difference time-domain (FDTD) calculations of the Au nanodisks optical response were performed by matching to the experimental extinction spectra and determined sensitivities, plotted in Figure 4. Experimental and FDTD spectra present similar peak shapes and positions although relative intensity is slightly different. Additionally, both spectra with peaks resulting from a dipole resonance are in good agreement, Figure 4A and B. FDTD simulations matched, as a starting point, the Au nanodisks dimensions of 100 nm diameter by 22 nm height (20 nm Au with 2 nm Ti adhesion layer) and the corresponding experimental extinction peak. The Au nanodisk modification led to an LSPR peak shift which is directly correlated with experimental bulk refractive index changes. The sensitivity to refractive index changes in thin films was measured by variation of the films refractive index in the FDTD model and assuming a maximum thickness of 7/14 nm for the AMY and saliva films, respectively. The obtained calibration curves for 7 and 14 nm films are plotted in Figure 4C and D. Measurements by SPR on homogeneous surfaces indicated a surface coverage of AMY consistent with a side on configuration of AMY with maximum footprint (AMY size is indicated to be 11.5 × 11.9 × 7.0 nm³) which points to an AMY thickness of 7 nm. Salivary proteins are known to form thicker layers,(41) and here we assumed that the layer thickness was 14 nm, roughly determined based on the protein composition of saliva and their three-dimensional size. The final refractive index of the saliva layer using calibration from FDTD simulations, assuming a 14 nm layer thickness, was 1.38 which fits well with the refractive indices measured on adsorbed saliva films.(41)

FDTD also provided additional information about the spatial confinement of the plasmon induced near–field, which indicates that highest values of the near-field enhancement of the incoming optical field are localized around the upper and lower rims of the Au nanodisk, as can be seen in Figure 4E. The outcome of FDTD calculations allows the quantification of the rebinding of protein and the amount of interacting polyphenols.

Binding Affinities

In this work, we carry out proof of principle studies of the interaction of different polyphenol compounds with the complex saliva MIP. Polyphenols from different classes, flavonoid and nonflavonoid, were tested. Three polyphenols were selected for the binding affinity studies: PGG from the nonflavonoid class consisting of a glucose molecule esterified with five gallic acid and two different structural catechins; (+)-catechin and procyanidin dimer B3 [(+)-catechin-(4–8)-(+)-catechin].

Each polyphenol was injected in the flow system interacting with the protein content on both AIM and SIM surfaces, while control NIP and AIM/SIM without protein rebinding were also evaluated. Generally, the imprinted materials provided better response than nonimprinted materials, Figure S-7, Supporting Information. Additionally, the obtained signals when using saliva are significantly higher than those for the tests with AMY. The imprinted material with no rebinding was used as a control providing the lower signal (Table S-6 and Figure S-7 in the Supporting Information). Binding characteristics were measured by repeated injection of increasing concentrations of PGG ranging 0.1–955 μM, catechin 160–56 500 μM, and B3 100–57 000 μM, all shown in Figure 5.

When PGG, catechin or B3 were injected in the system, they interacted with surface bound protein and gave red shifts of the plasmon peak that remained after rinsing indicating a strong interaction. The obtained shifts indicate a linear dependence with log Polyphenol concentration (LSPR λ_max shift vs log concentration). Though, for all polyphenols, the linear response was only achieved for a smaller region within the tested concentration range.

The signal from PGG binding to the LSPR sensor surface (Figure S-7, Supporting Information) showed a consistently higher binding at MIP surfaces compared to NIP. The difference was much larger for saliva surfaces compared to AMY surfaces, which correlated to an overall lower protein binding of the AMY. The variation in the measurements for the NIP surfaces was substantially larger than MIP surfaces that may result from weaker or more variable protein-NIP surface interactions. Binding of polyphenols directly to the polymer surface in the absence of protein, showed a low but significant level. When protein is attached to the surface (in particular for the saliva surfaces) it likely reduces this background binding both competing for PGG adsorption and blocking the surface. We correlate the PGG binding to the amount of protein in order to estimate the binding characteristics. The quantification for the AMY assumed a 7 nm layer while that of the saliva used a 14 nm layer. It should be noted that the ratio of the amount of polyphenol to protein is unaffected by the assumed thickness. In Figure 5A, the ratio of polyphenol mass/protein mass is plotted versus polyphenol concentration (log scale). This mass ratio can be indirectly corrected with the peak shift through the refractive index increment which is higher by a factor of 3 for PGG (0.532 cm²/g experimentally measured value) in comparison with the protein (0.180 cm²/g literature value(42)). PGG binding to saliva is higher than binding to AMY (∼2 times higher). We cannot rule out a contribution of PGG binding directly to the MIP surface; however, the PGG binding to AMY corresponds to around 20–25 PGGs/protein for the highest concentration which is comparable to that previously observed for PGG binding to AMY covalently attached to surfaces.(32) The stronger PGG attachment to the complex protein mixture of saliva (we observe more than 36 proteins at the MIP layer by mass spectrometry including AMY; see Table S-7 in the Supporting Information) indicates that other proteins within the saliva are significantly stronger binders for PGG than AMY, suggesting that sensors based on specific single proteins (even those which are the most abundant) risk wrongly evaluating the global response. The binding profiles for PGG showed a linear regime (in the log scale) at higher concentrations but with significant deviations toward higher binding at low concentrations suggesting that there are ranges of binding strength sites at the proteins (which has been observed before for PGG binding to AMY). The overall amount of PGG molecules binding reaches a very high level at higher concentrations at the saliva. While we cannot calculate the number of PGG molecules binding to each protein in saliva we estimate the binding to an AMY sized protein would on average be ∼40 which indicates that protein unfolding reveals additional binding sites or that PGG cluster growth occurs at already bound PGG molecules.

We applied our sensing approach to study the differences between polyphenol interaction with proteins. The combination of ultrathin MIP layer with LSPR allowed us to evaluate the binding of two small polyphenols (the monomeric basic unit of condensed tannins, (+)-catechin MW 290.3, and a catechin dimer, the procyanin-B3 MW 2 × 290.3) and the PGG (MW 940.7), with both AMY and saliva.

The LSPR signals for B3 (Figure S-7B, Supporting Information) and catechin (Figure S-7C, Supporting Information) were significantly lower compared to that for the PGG as might be expected from their lower molecular weight; however, significantly larger concentrations of the polyphenols were required to induce binding, indicating a concomitant weaker interaction (see Figure 5). Binding to the polymer surface in the absence of the protein was also significantly lower than for PGG. Interestingly, the two smaller polyphenols studied showed different profiles of binding to AMY versus saliva. B3 binding to AMY was stronger (∼factor of 2) than to the complex saliva protein mixture and higher binding tendency with the increase of B3 concentration. While for catechin the binding to AMY is higher than to the saliva complex but with similar binding tendency with increased catechin concentration, also suggesting a stronger interaction. This fact could indicate that AMY has a limited number of higher binding sites while the complex of saliva proteins has some proteins with substantial numbers of low binding strength sites. The signal levels observed for the catechin binding with its low molecular weight to AMY were similar to those for the maximal binding observed at nonprotein covered surface (albeit at higher concentrations of catechin) and with significant errors indicating that the catechin binding to AMY is likely close to the detection limit for our system.

Overall, we observed a significant variation in the binding strength of polyphenols to the complex mixture of saliva proteins compared to binding to one specific protein (AMY). Amylase is shown to bind PGG weakly relative to saliva but to bind B3 and catechin stronger. This demonstrates that for studying global effects of different small molecule binding on proteins, a complex saliva protein mixture has the potential to give a better response than sensors based on single or a few proteins. For polyphenol binding to the complex saliva mixture, we observe a strong variation in binding of specific polyphenols. The effect of a complex food matrix on the protein and polyphenol interaction was also tested showing some interference, although the signal was affected in a very systematic way indicating that for the analysis of complex food matrices a careful choice of an appropriated matrix for calibration needs to be made (Figure S-8, Supporting Information). In the field of food science, this provides a method and proof of principle to study quantitatively both the importance of different polyphenols in astringency but also to understand and correct for the astringency response from specific wines and base ingredients during production. In particular, these approaches may be used to study the bioavailability of polyphenols from food and beverages after passing through the oral environment. A similar concept for studying global binding response of drug molecules to the complex protein environment of tumors or intracellular environment could be applied to estimate retention or local bioavailability of drug molecules in therapeutic situations on the site of action.

The presented results indicate that all three polyphenols showed large affinity with proteins and may interact with multiple binding sites. The binding affinity provides information about barriers to polyphenol transport through interaction with complex protein matrices before its absorption by the organism and consequently about their bioavailability. According to these results it seems that PGG will be the less available polyphenol after passing through the mouth while catechin will be the most available. Catechin is a monomer with low molecular size which may favor its absorption by the intestine lumen.

Conclusions

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Here we have developed a plasmonic biosensor to study global interactions between small molecules and complex protein matrices. We have made use of smart MIP layers which are ultrathin, combining with the high localization of the optical fields around the plasmonic sensor and imprint complex protein matrices to allow the capture and study of saliva and its interaction with polyphenols. The sensor would allow the study of bioavailability of small molecules in food or drug delivery applications associated with a broad range of disorders including neurodegenerative diseases, cardiovascular disease, and cancer.

Supporting Information

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The Supporting Information is available free of charge on the ACS Publications website at DOI: 10.1021/acssensors.5b00054.

Materials and methods including saliva characterization, Au nanodisks fabrication, molecular imprinted synthesis, and evaluation, interaction measurements by LSPR, electrochemical measurements, as well as description of data analysis; bare Au disks MIP and nonimprinted layer characterized by atomic force microscopy; mass spectroscopy of both pure saliva and Au disks/MIP saliva/rebinding saliva (PDF)

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Author Contributions

The manuscript was written through contributions of all authors. All authors have given approval to the final version of the manuscript.

The authors declare no competing financial interest.

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Acknowledgment

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The authors acknowledge FCT, Fundação para a Ciência e Tecnologia, for the financial support (SFRH/BD/72479/2010), the FSE, Fundo Social Europeu for the cofinancial support. Vladimir Bochenkov acknowledges the support from RFBR Grant #15-03-99582.

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A review. The formation of well-ordered fibrillar protein deposits is common to a large group of amyloid-assocd. disorders. This group consists of several major human diseases such as Alzheimer's disease, Parkinson's disease, prion diseases, and type II diabetes. Currently, there is no approved therapeutic agent directed towards the formation of fibrillar assemblies, which have been recently shown to have a key role in the cytotoxic nature of amyloidogenic proteins. One important approach in the development of therapeutic agents is the use of small mols. that specifically and efficiently inhibit the aggregation process. Several small polyphenol mols. have been demonstrated to remarkably inhibit the formation of fibrillar assemblies in vitro and their assocd. cytotoxicity. Yet, the inhibition mechanism was mostly attributed to the antioxidative properties of these polyphenol compds. Based on several observations demonstrating that polyphenols are capable of inhibiting amyloid fibril formation in vitro, regardless of oxidative conditions, and in view of their structural similarities, we suggest an addnl. mechanism of action. This mechanism is assuming structural constraints and specific arom. interactions, which direct polyphenol inhibitors to the amyloidogenic core. This proposed mechanism is highly relevant for future de novo inhibitors' design as therapeutic agents for the treatment of amyloid-assocd. diseases.
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Corder, R.; Mullen, W.; Khan, N. Q.; Marks, S. C.; Wood, E. G.; Carrier, M. J.; Crozier, A. Red wine procyanidins and vascular health Nature 2006, 444, 566– 566 DOI: 10.1038/444566a
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Oenology: Red wine procyanidins and vascular health
Corder, R.; Mullen, W.; Khan, N. Q.; Marks, S. C.; Wood, E. G.; Carrier, M. J.; Crozier, A.
Nature (London, United Kingdom) (2006), 444 (7119), 566CODEN: NATUAS; ISSN:0028-0836. (Nature Publishing Group)
The relationship between procyanidin content and vasoactive properties of red wine was investigated in endothelial cell cultures. Total polyphenol and straight-chain B-type oligomeric procyanidin content correlated with the suppression of endothelin-1 synthesis. Wines produced in different countries including areas of increased longevity were compared. Wines from southwest France and a Sardinia region had 2-4-fold more biol. activity and procyanidin content due to traditional winemaking.
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Corder, R.; Douthwaite, J. A.; Lees, D. M.; Khan, N. Q.; Viseu dos Santos, A. C.; Wood, E. G.; Carrier, M. J. Endothelin-1 synthesis reduced by red wine - Red wines confer extra benefit when it comes to preventing coronary heart disease Nature 2001, 414, 863– 864 DOI: 10.1038/414863a
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Endothelin-1 synthesis reduced by red wine
Corder, Roger; Douthwaite, Julie A.; Lees, Delphine M.; Khan, Noorafza Q.; Viseu dos Santos, Ana Carolina; Wood, Elizabeth G.; Carrier, Martin J.
Nature (London, United Kingdom) (2001), 414 (6866), 863-864CODEN: NATUAS; ISSN:0028-0836. (Nature Publishing Group)
Ethanol-free exts. from 23 red wines, four white wines, one rose wine and one red grape juice were prepd. to det. their inhibitory effect on the synthesis of endothelin-1 (ET-1), a vasoactive peptide that is crucial in the development of coronary atherosclerosis. The degree of inhibition of ET-1 by red wine was correlated with its total phenol content. The red-grape juice did not significantly inhibit ET-1 synthesis, while no effect was obsd. with white and rose wine. The polyphenol content of the red wines were responsible for their inhibitory effect on ET-1 synthesis. The red wine ext. caused a significant change in the cell morphol. and a redistribution of phosphotyrosine staining. These effects on tyrosine phosphorylation were due to the modified tyrosine-kinase signaling in endothelial cells. Thus, moderate intake of red wine can prevent coronary heart disease.
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Fito, M.; Cladellas, M.; de la Torre, R.; Marti, J.; Munoz, D.; Schroder, H.; Alcantara, M.; Pujadas-Bastardes, M.; Marrugat, J.; Lopez-Sabater, M. C.; Bruguera, J.; Covas, M. I. Anti-inflammatory effect of virgin olive oil in stable coronary disease patients: a randomized, crossover, controlled trial Eur. J. Clin. Nutr. 2008, 62, 570– 574 DOI: 10.1038/sj.ejcn.1602724
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Anti-inflammatory effect of virgin olive oil in stable coronary disease patients: a randomized, crossover, controlled trial
Fito, M.; Cladellas, M.; de la Torre, R.; Marti, J.; Munoz, D.; Schroeder, H.; Alcantara, M.; Pujadas-Bastardes, M.; Marrugat, J.; Lopez-Sabater, M. C.; Bruguera, J.; Covas, M. I.
European Journal of Clinical Nutrition (2008), 62 (4), 570-574CODEN: EJCNEQ; ISSN:0954-3007. (Nature Publishing Group)
Objectives: To assess the effect of two similar olive oils, but with differences in their phenolic compds. (powerful antioxidant compds.), on inflammatory markers in stable coronary heart disease patients. Design: Placebo-controlled, crossover, randomized trial. Setting: Cardiol. Department of Hospital del Mar and Institut Municipal d'Investigacio Medica (Barcelona). Subjects: Twenty-eight stable coronary heart disease patients. Interventions: A raw daily dose of 50 mL of virgin and refined olive oil (ROO) was sequentially administered over two periods of 3-wk, preceded by 2-wk washout periods in which ROO was used. Results: Interleukin-6 (P<0.002) and C-reactive protein (P=0.024) decreased after virgin olive oil intervention. No changes were obsd. in sol. intercellular and vascular adhesion mols., glucose and lipid profile. Conclusions: Consumption of virgin olive oil, could provide beneficial effects in stable coronary heart disease patients as an addnl. intervention to the pharmacol. treatment.
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7
Gescher, A.; Pastorino, U.; Plummer, S. M.; Manson, M. M. Suppression of tumour development by substances derived from the diet - mechanisms and clinical implications Br. J. Clin. Pharmacol. 1998, 45, 1– 12 DOI: 10.1046/j.1365-2125.1998.00640.x
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Suppression of tumor development by substances derived from the diet - mechanisms and clinical implications
Gescher, Andreas; Pastorino, Ugo; Plummer, Simon M.; Manson, Margaret M.
British Journal of Clinical Pharmacology (1998), 45 (1), 1-12CODEN: BCPHBM; ISSN:0306-5251. (Blackwell Science Ltd.)
A review with 99 refs. The concept that cancer can be prevented, or its onset postponed, by certain diet-derived substances is eliciting considerable interest. Agents which interfere with tumor promotion and progression are of potential clin. value. As chemopreventive agents have to be administered over a long period of time to establish whether they possess efficacy in humans, it is important to establish their lack of toxicity. The desire to select the best drug candidates for clin. trials and the necessity to monitor efficacy in the short and intermediate terms give the identification of specific mechanism-based in vivo markers of biol. activity a high priority. Antioxidn., inhibition of arachidonic acid metab., modulation of cellular signal transduction pathways, inhibition of hormone and growth factor activity, and inhibition of oncogene activity are discussed as mechanisms by which the soybean constituent genistein, the curry ingredient curcumin, and the vitamin A analog 13-cis-retinoic acid exert their tumor suppression activity. Better understanding of the mechanisms will help to screen and discover new chemopreventive agents and to identify surrogate markers to assess the outcome of clin. chemoprevention trials.
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Middleton, E.; Kandaswami, C.; Theoharides, T. C. The effects of plant flavonoids on mammalian cells: Implications for inflammation, heart disease, and cancer Pharmacol. Rev. 2000, 52, 673– 751
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The effects of plant flavonoids on mammalian cells: Implications for inflammation, heart disease, and cancer
Middleton, Elliott, Jr.; Kandaswami, Chithan; Theoharides, Theoharis C.
Pharmacological Reviews (2000), 52 (4), 673-751CODEN: PAREAQ; ISSN:0031-6997. (American Society for Pharmacology and Experimental Therapeutics)
A review with about 1000 refs. Flavonoids are nearly ubiquitous in plants and are recognized as the pigments responsible for the colors of leaves, esp. in autumn. They are rich in seeds, citrus fruits, olive oil, tea, and red wine. They are low mol. wt. compds. composed of a three-ring structure with various substitutions. This basic structure is shared by tocopherols (vitamin E). Flavonoids can be subdivided according to the presence of an oxy group at position 4, a double bond between carbon atoms 2 and 3, or a hydroxyl group in position 3 of the C (middle) ring. These characteristics appear to also be required for best activity, esp. antioxidant and antiproliferative, in the systems studied. The particular hydroxylation pattern of the B ring of the flavonoles increases their activities, esp. in inhibition of mast cell secretion. Certain plants and spices contg. flavonoids have been used for thousands of years in traditional Eastern medicine. In spite of the voluminous literature available, however, Western medicine has not yet used flavonoids therapeutically, even though their safety record is exceptional. Suggestions are made where such possibilities may be worth pursuing.
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Aggarwal, B. B.; Shishodia, S. Molecular targets of dietary agents for prevention and therapy of cancer Biochem. Pharmacol. 2006, 71, 1397– 1421 DOI: 10.1016/j.bcp.2006.02.009
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Molecular targets of dietary agents for prevention and therapy of cancer
Aggarwal, Bharat B.; Shishodia, Shishir
Biochemical Pharmacology (2006), 71 (10), 1397-1421CODEN: BCPCA6; ISSN:0006-2952. (Elsevier B.V.)
A review. While fruits and vegetables are recommended for prevention of cancer and other diseases, their active ingredients (at the mol. level) and their mechanisms of action less well understood. Extensive research during the last half century has identified various mol. targets that can potentially be used not only for the prevention of cancer but also for treatment. However, lack of success with targeted monotherapy resulting from bypass mechanisms has forced researchers to employ either combination therapy or agents that interfere with multiple cell-signaling pathways. In this review, we present evidence that numerous agents identified from fruits and vegetables can interfere with several cell-signaling pathways. The agents include curcumin (turmeric), resveratrol (red grapes, peanuts, and berries), genistein (soybean), diallyl sulfide (allium), S-allyl cysteine (allium), allicin (garlic), lycopene (tomato), capsaicin (red chilli), diosgenin (fenugreek), 6-gingerol (ginger), ellagic acid (pomegranate), ursolic acid (apples, pears, prunes), silymarin (milk thistle), anethol (anise, camphor, and fennel), catechins (green tea), eugenol (cloves), indole-3-carbinol (cruciferous vegetables), limonene (citrus fruits), β-carotene (carrots), and dietary fiber. For instance, the cell-signaling pathways inhibited by curcumin alone include NF-κB, AP-1, STAT3, Akt, Bcl-2, Bcl-XL, caspases, PARP, IKK, EGFR, HER2, JNK, MAPK, COX2, and 5-LOX. The active principle identified in fruit and vegetables and the mol. targets modulated may be the basis for how these dietary agents not only prevent but also treat cancer and other diseases. This work reaffirms what Hippocrates said 25 centuries ago, let food be thy medicine and medicine be thy food.
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Daglia, M. Polyphenols as antimicrobial agents Curr. Opin. Biotechnol. 2012, 23, 174– 181 DOI: 10.1016/j.copbio.2011.08.007
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Polyphenols as antimicrobial agents
Daglia, Maria
Current Opinion in Biotechnology (2012), 23 (2), 174-181CODEN: CUOBE3; ISSN:0958-1669. (Elsevier B.V.)
A review. Polyphenols are secondary metabolites produced by higher plants, which play multiple essential roles in plant physiol. and have potential healthy properties on human organism, mainly as antioxidants, anti-allergic, anti-inflammatory, anticancer, antihypertensive, and antimicrobial agents. In the present review the antibacterial, antiviral, and antifungal activities of the most active polyphenol classes are reported, highlighting, where investigated, the mechanisms of action and the structure-activity relationship. Moreover, considering that the microbial resistance has become an increasing global problem, and there is a compulsory need to find out new potent antimicrobial agents as accessories to antibiotic therapy, the synergistic effect of polyphenols in combination with conventional antimicrobial agents against clin. multidrug-resistant microorganisms is discussed.
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Ferrazzano, G. F.; Amato, I.; Ingenito, A.; Zarrelli, A.; Pinto, G.; Pollio, A. Plant Polyphenols and Their Anti-Cariogenic Properties: A Review Molecules 2011, 16, 1486– 1507 DOI: 10.3390/molecules16021486
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Plant polyphenols and their anti-cariogenic properties: a review
Ferrazzano, Gianmaria F.; Amato, Ivana; Ingenito, Aniello; Zarrelli, Armando; Pinto, Gabriele; Pollio, Antonino
Molecules (2011), 16 (), 1486-1507CODEN: MOLEFW; ISSN:1420-3049. (MDPI AG)
A review. Polyphenols constitute one of the most common groups of substances in plants. Polyphenolic compds. have been reported to have a wide range of biol. activities, many of which are related to their conventional antioxidant action; however, increasing scientific knowledge has highlighted their potential activity in preventing oral disease, including the prevention of tooth decay. The aim of this review is to show the emerging findings on the anti-cariogenic properties of polyphenols, which have been obtained from several in vitro studies investigating the effects of these bioactive mols. against Streptococcus mutans, as well as in vivo studies. The anal. of the literature supports the anti-bacterial role of polyphenols on cariogenic streptococci, suggesting (1) a direct effect against S. mutans; (2) an interaction with microbial membrane proteins inhibiting the adherence of bacterial cells to the tooth surface; and (3) the inhibition of glucosyl transferase and amylase. However, more studies, particularly in vivo and in situ, are necessary to establish conclusive evidence for the effectiveness and the clin. applications of these compds. in the prevention of dental caries. It is essential to better det. the nature and distribution of these compds. in our diet and to identify which of the hundreds of existing polyphenols are likely to provide the greatest effects.
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Link, A.; Balaguer, F.; Goel, A. Cancer chemoprevention by dietary polyphenols: Promising role for epigenetics Biochem. Pharmacol. 2010, 80, 1771– 1792 DOI: 10.1016/j.bcp.2010.06.036
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Cancer chemoprevention by dietary polyphenols: Promising role for epigenetics
Link, Alexander; Balaguer, Francesc; Goel, Ajay
Biochemical Pharmacology (2010), 80 (12), 1771-1792CODEN: BCPCA6; ISSN:0006-2952. (Elsevier B.V.)
A review. Epigenetics refers to heritable changes that are not encoded in the DNA sequence itself, but play an important role in the control of gene expression. In mammals, epigenetic mechanisms include changes in DNA methylation, histone modifications and non-coding RNAs. Although epigenetic changes are heritable in somatic cells, these modifications are also potentially reversible, which makes them attractive and promising avenues for tailoring cancer preventive and therapeutic strategies. Burgeoning evidence in the last decade has provided unprecedented clues that diet and environmental factors directly influence epigenetic mechanisms in humans. Dietary polyphenols from green tea, turmeric, soybeans, broccoli and others have shown to possess multiple cell-regulatory activities within cancer cells. More recently, we have begun to understand that some of the dietary polyphenols may exert their chemopreventive effects in part by modulating various components of the epigenetic machinery in humans. In this article, the authors 1st discuss the contribution of diet and environmental factors on epigenetic alterations; subsequently, the authors provide a comprehensive review of literature on the role of various dietary polyphenols. In particular, we summarize the current knowledge on a large no. of dietary agents and their effects on DNA methylation, histone modifications and regulation of expression of the non-coding miRNAs in various in vitro and in vivo models. We emphasize how increased understanding of the chemopreventive effects of dietary polyphenols on specific epigenetic alterations may provide unique and yet unexplored novel and highly effective chemopreventive strategies for reducing the health burden of cancer and other diseases in humans.
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Izzotti, A.; Cartiglia, C.; Steele, V. E.; De Flora, S. MicroRNAs as targets for dietary and pharmacological inhibitors of mutagenesis and carcinogenesis Mutat. Res., Rev. Mutat. Res. 2012, 751, 287– 303 DOI: 10.1016/j.mrrev.2012.05.004
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MicroRNAs as targets for dietary and pharmacological inhibitors of mutagenesis and carcinogenesis
Izzotti, Alberto; Cartiglia, Cristina; Steele, Vernon E.; De Flora, Silvio
Mutation Research, Reviews in Mutation Research (2012), 751 (2), 287-303CODEN: MRRRFK; ISSN:1383-5742. (Elsevier B.V.)
A review. MicroRNAs (miRNAs) have been implicated in many biol. processes, cancer, and other diseases. In addn., miRNAs are dysregulated following exposure to toxic and genotoxic agents. Here we review studies evaluating modulation of miRNAs by dietary and pharmacol. agents, which could potentially be exploited for inhibition of mutagenesis and carcinogenesis. This review covers natural agents, including vitamins, oligoelements, polyphenols, isoflavones, indoles, isothiocyanates, phospholipids, saponins, anthraquinones and polyunsatd. fatty acids, and synthetic agents, including thiols, nuclear receptor agonists, histone deacetylase inhibitors, antiinflammatory drugs, and selective estrogen receptor modulators. As many as 145 miRNAs, involved in the control of a variety of carcinogenesis mechanisms, were modulated by these agents, either individually or in combination. Most studies used cancer cells in vitro with the goal of modifying their phenotype by changing miRNA expression profiles. In vivo studies evaluated regulation of miRNAs by chemopreventive agents in organs of mice and rats, either untreated or exposed to carcinogens, with the objective of evaluating their safety and efficacy. The tissue specificity of miRNAs could be exploited for the chemoprevention of site-specific cancers, and the study of polymorphic miRNAs is expected to predict the individual response to chemopreventive agents as a tool for developing new prevention strategies.
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Li, Y. Y.; Zhang, T. Targeting cancer stem cells by curcumin and clinical applications Cancer Lett. 2014, 346, 197– 205 DOI: 10.1016/j.canlet.2014.01.012
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Targeting cancer stem cells by curcumin and clinical applications
Li, Yanyan; Zhang, Tao
Cancer Letters (New York, NY, United States) (2014), 346 (2), 197-205CODEN: CALEDQ; ISSN:0304-3835. (Elsevier)
A review. Curcumin is a well-known dietary polyphenol derived from the rhizomes of turmeric, an Indian spice. The anticancer effect of curcumin has been demonstrated in many cell and animal studies, and recent research has shown that curcumin can target cancer stem cells (CSCs). CSCs are proposed to be responsible for initiating and maintaining cancer, and contribute to recurrence and drug resistance. A no. of studies have suggested that curcumin has the potential to target CSCs through regulation of CSC self-renewal pathways (Wnt/β-catenin, Notch, sonic hedgehog) and specific microRNAs involved in acquisition of epithelial-mesenchymal transition (EMT). The potential impact of curcumin, alone or in combination with other anticancer agents, on CSCs was evaluated as well. Furthermore, the safety and tolerability of curcumin have been well-established by numerous clin. studies. Importantly, the low bioavailability of curcumin has been dramatically improved through the use of structural analogs or special formulations. More clin. trials are underway to investigate the efficacy of this promising agent in cancer chemoprevention and therapy. In this article, we review the effects of curcumin on CSC self-renewal pathways and specific microRNAs, as well as its safety and efficacy in recent human studies. In conclusion, curcumin could be a very promising adjunct to traditional cancer treatments.
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Santangelo, C.; Vari, R.; Scazzocchio, B.; Di Benedetto, R.; Filesi, C.; Masella, R. Polyphenols, intracellular signalling and inflammation Ann. Ist. Super. Sanita 2007, 43, 394– 405
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Polyphenols, intracellular signalling and inflammation
Santangelo, Carmela; Vari, Rosaria; Scazzocchio, Beatrice; Di Benedetto, Roberta; Filesi, Carmela; Masella, Roberta
Annali dell'Istituto Superiore di Sanita (2007), 43 (4), 394-405CODEN: AISSAW; ISSN:0021-2571. (Istituto Superiore di Sanita)
A review. Excessive inflammation is considered as a crit. factor in many human diseases, including cancer, obesity, type II diabetes, cardiovascular diseases, neurodegenerative diseases and aging. Compds. derived from botanic sources, such as phenolic compds., have shown anti-inflammatory activity in vitro and in vivo. Recent data suggest that polyphenols can work as modifiers of signal transduction pathways to elicit their beneficial effects. These natural compds. express anti-inflammatory activity by modulation of pro-inflammatory gene expression such as cyclooxygenase, lipoxygenase, nitric oxide synthases and several pivotal cytokines, mainly by acting through nuclear factor-kappa B and mitogen-activated protein kinase signalling. This review will discuss recent data on the control of inflammatory signalling exerted by some dietary polyphenols contained in Mediterranean diet. A clear understanding of the mol. mechanisms of action of phenolic compds. is crucial in the valuation of these potent mols. as potential prophylactic and therapeutic agents.
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Albini, A.; Tosetti, F.; Li, V. W.; Noonan, D. M.; Li, W. W. Cancer prevention by targeting angiogenesis Nat. Rev. Clin. Oncol. 2012, 9, 498– 509 DOI: 10.1038/nrclinonc.2012.120
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Cancer prevention by targeting angiogenesis
Albini, Adriana; Tosetti, Francesca; Li, Vincent W.; Noonan, Douglas M.; Li, William W.
Nature Reviews Clinical Oncology (2012), 9 (9), 498-509CODEN: NRCOAA; ISSN:1759-4774. (Nature Publishing Group)
A review. Healthy individuals can harbor microscopic tumors and dysplastic foci in different organs in an undetectable and asymptomatic state for many years. These lesions do not progress in the absence of angiogenesis or inflammation. Targeting both processes before clin. manifestation can prevent tumor growth and progression. Angioprevention is a chemoprevention approach that interrupts the formation of new blood vessels when tumor cell foci are in an indolent state. Many efficacious chemopreventive drugs function by preventing angiogenesis in the tumor microenvironment. Blocking the vascularization of incipient tumors should maintain a dormancy state such that neoplasia or cancer exist without disease. The current limitations of antiangiogenic cancer therapy may well be related to the use of antiangiogenic agents too late in the disease course. In this Review, we suggest mechanisms and strategies for using antiangiogenesis agents in a safe, preventive clin. angioprevention setting, proposing different levels of clin. angioprevention according to risk, and indicate potential drugs to be employed at these levels. Finally, angioprevention may go well beyond cancer in the prevention of a range of chronic disorders where angiogenesis is crucial, including different forms of inflammatory or autoimmune diseases, ocular disorders, and neurodegeneration.
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Potapovich, A. I.; Lulli, D.; Fidanza, P.; Kostyuk, V. A.; De Luca, C.; Pastore, S.; Korkina, L. G. Plant polyphenols differentially modulate inflammatory responses of human keratinocytes by interfering with activation of transcription factors NF kappa B and AhR and EGFR-ERK pathway Toxicol. Appl. Pharmacol. 2011, 255, 138– 149 DOI: 10.1016/j.taap.2011.06.007
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Plant polyphenols differentially modulate inflammatory responses of human keratinocytes by interfering with activation of transcription factors NFκB and AhR and EGFR-ERK pathway
Potapovich, Alla I.; Lulli, Daniela; Fidanza, Paolo; Kostyuk, Vladimir A.; De Luca, Chiara; Pastore, Saveria; Korkina, Liudmila G.
Toxicology and Applied Pharmacology (2011), 255 (2), 138-149CODEN: TXAPA9; ISSN:0041-008X. (Elsevier B.V.)
Mol. mechanisms underlying modulation of inflammatory responses in primary human keratinocytes by plant polyphenols (PPs), namely the glycosylated phenylpropanoid verbascoside, the stilbenoid resveratrol and its glycoside polydatin, and the flavonoid quercetin and its glycoside rutin were evaluated. As non-lethal stimuli, the prototypic ligand for epidermal growth factor receptor (EGFR) transforming growth factor alpha (TGFalpha), the combination of tumor necrosis factor (TNFalpha) and interferon (IFNgamma) (T/I), UVA + UVB irradn., and bacterial lipopolysaccharide (LPS) were used. We demonstrated differential modulation of inflammatory responses in keratinocytes at signal transduction, gene transcription, and protein synthesis levels as a function of PP chem. structure, the pro-inflammatory trigger used, and PP interaction with intracellular detoxifying systems. The PPs remarkably inhibited constitutive, LPS- and T/I-induced but not TGFalpha-induced ERK phosphorylation. They also suppressed NFkappaB activation by LPS and T/I. Verbascoside and quercetin invariably impaired EGFR phosphorylation and UV-assocd. aryl hydrocarbon receptor (AhR)-mediated signaling, while rutin, polydatin and resveratrol did not affect EGFR phosphorylation and further activated AhR machinery in UV-exposed keratinocytes. In general, PPs down-regulated gene expression of pro-inflammatory cytokines/enzymes, except significant up-regulation of IL-8 obsd. under stimulation with TGFalpha. Both spontaneous and T/I-induced release of IL-8 and IP-10 was suppressed, although 50 μM resveratrol and polydatin up-regulated IL-8. At this concn., resveratrol activated both gene expression and de novo synthesis of IL-8 and AhR-mediated mechanisms were involved. We conclude that PPs differentially modulate the inflammatory response of human keratinocytes through distinct signal transduction pathways, including AhR and EGFR.
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Sinclair, D. A.; Guarente, L. Small-Molecule Allosteric Activators of Sirtuins. In Annual Review of Pharmacology and Toxicology, Vol 54; Insel, P. A., Ed.; Annual Reviews: Palo Alto, CA, 2014; Vol. 54, pp 363– 380.
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Surh, Y. J. Cancer chemoprevention with dietary phytochemicals Nat. Rev. Cancer 2003, 3, 768– 780 DOI: 10.1038/nrc1189
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Cancer chemoprevention with dietary phytochemicals
Surh, Young-Joon
Nature Reviews Cancer (2003), 3 (10), 768-780CODEN: NRCAC4; ISSN:1474-175X. (Nature Publishing Group)
A review. Chemoprevention refers to the use of agents to inhibit, reverse or retard tumorigenesis. Numerous phytochems. derived from edible plants have been reported to interfere with a specific stage of the carcinogenic process. Many mechanisms have been shown to account for the anticarcinogenic actions of dietary constituents, but attention has recently been focused on intracellular-signaling cascades as common mol. targets for various chemopreventive phytochems.
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Ramos, S. Cancer chemoprevention and chemotherapy: Dietary polyphenols and signalling pathways Mol. Nutr. Food Res. 2008, 52, 507– 526 DOI: 10.1002/mnfr.200700326
[ Crossref], [ PubMed], [ CAS], Google Scholar
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Cancer chemoprevention and chemotherapy: dietary polyphenols and signalling pathways
Ramos, Sonia
Molecular Nutrition & Food Research (2008), 52 (5), 507-526CODEN: MNFRCV; ISSN:1613-4125. (Wiley-VCH Verlag GmbH & Co. KGaA)
A review. Prevention of cancer through dietary intervention recently has received an increasing interest, and dietary polyphenols have become not only important potential chemopreventive, but also therapeutic, natural agents. Polyphenols have been reported to interfere at the initiation, promotion and progression of cancer. They might lead to the modulation of proteins in diverse pathways and require the integration of different signals for the final chemopreventive or therapeutic effect. Polyphenols have been demonstrated to act on multiple key elements in signal transduction pathways related to cellular proliferation, differentiation, apoptosis, inflammation, angiogenesis and metastasis; however, these mol. mechanisms of action are not completely characterized and many features remain to be elucidated. The aim of this review is to provide insights into the mol. basis of potential chemopreventive and therapeutic activities of dietary polyphenols with emphasis in their ability to control intracellular signaling cascades considered as relevant targets in a cancer preventive approach.
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Seeram, N. P.; Zhang, Y. J.; Nair, M. G. Inhibition of proliferation of human cancer cells and cyclooxygenase enzymes by anthocyanidins and catechins Nutr. Cancer 2003, 46, 101– 106 DOI: 10.1207/S15327914NC4601_13
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Inhibition of proliferation of human cancer cells and cyclooxygenase enzymes by anthocyanidins and catechins
Seeram, Navindra P.; Zhang, Yanjun; Nair, Muraleedharan G.
Nutrition and Cancer (2003), 46 (1), 101-106CODEN: NUCADQ; ISSN:0163-5581. (Lawrence Erlbaum Associates, Inc.)
The widespread consumption of diets rich in anthocyanin and catechin content prompted the evaluation of their in vitro inhibitory effects on cyclooxygenase (COX) enzymes and on the proliferation of human cancer cell lines. Five anthocyanidins consisting of cyanidin (1), delphinidin (2), pelargonidin (3), peonidin (4), and malvidin (5) were tested for COX-1 and -2 enzyme inhibitory activities at 40 μM. Eleven catechins consisting of (+)-catechin (6), (-)-catechin (7), (±)-catechin (8), (+)-epicatechin (9), (-)-epicatechin (10), (-)-epigallocatechin (11), (-)-gallocatechin (12), (-)-epicatechin gallate (13), (-)-catechin gallate (14), (-)-epigallocatechin gallate (15), and (-)-gallocatechin gallate (16) were tested for inhibitory effects of COX-1 and -2 enzymes at 80 μM. Of the compds. tested, the galloyl derivs. of the catechins 11-15, cyanidin and malvidin , showed the best COX inhibitory activities compared with the com. anti-inflammatory drugs ibuprofen (at 10 μM), naproxen (at 10 μM), Vioxx (at 1.67 ppm), and Celebrex (at 1.67 ppm). Inhibition of the proliferation of the human cancer cell lines MCF-7 (breast), SF-268 (central nervous system, CNS), HCT-116 (colon), and NCI-H460 (lung) was evaluated at concns. between 100 and 6.25 μM compared with the com. std., adriamycin (doxorubicin) at 6.25 μM. At 100-μM concns., anthocyanidins 1-5 and catechins 6-10 did not inhibit proliferation of the four cell lines. At 50-μM concns., catechins 12, 15, and 16 showed 95%, 100%, and 97% inhibition of breast cells, resp. At 50-μM concns. 12 and 16 were the most effective catechins against colon cells (85% and 93%, resp.) and lung cells (87% and 67%, resp.). CNS cells were the most sensitive of the test cell lines, and total growth inhibition was obtained with catechins 12 and 16 at 100-μM concns. Overall, only the galloyl derivs. of catechins 11-16 inhibited the proliferation of the cancer cell lines.
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Xagorari, A.; Roussos, C.; Papapetropoulos, A. Inhibition of LPS-stimulated pathways in macrophages by the flavonoid luteolin Br. J. Pharmacol. 2002, 136, 1058– 1064 DOI: 10.1038/sj.bjp.0704803
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Inhibition of LPS-stimulated pathways in macrophages by the flavonoid luteolin
Xagorari, Angeliki; Roussos, Charis; Papapetropoulos, Andreas
British Journal of Pharmacology (2002), 136 (7), 1058-1064CODEN: BJPCBM; ISSN:0007-1188. (Nature Publishing Group)
1 We have previously shown that the flavonoid luteolin inhibits the expression of pro-inflammatory mols. induced by LPS. In the present study we tested the ability of luteolin to block signaling pathways implicated in LPS-induced inflammatory gene expression in macrophages. 2 Exposure of the murine macrophage cell line RAW 264.7 to LPS increased phosphorylation of the mitogen-activated protein kinase family members ERK1/2, p38 and JNK1/2 in a time-dependent manner. Pretreatment of RAW 264.7 with luteolin inhibited the LPS-induced ERK1/2 and p38, but not JNK1/2, phosphorylation, and blocked the LPS-induced TNF-α release. 3 To investigate which of these pathways contribute to the inhibitory effects of luteolin on TNF-α release, cells were pretreated with pharmacol. inhibitors of these pathways; PD98059 and SB203580 when used alone failed to inhibit TNF-α release, whereas pretreatment with both agents attenuated TNF-α release. 4 We have previously shown that luteolin blocks Akt phosphorylation in response to LPS in RAW 264.7 macrophages. To det. the role of Akt in TNF-α release, cells were transiently transfected with a dominant neg. form of Akt (K179M). Overexpression of K179M Akt did not alter LPS-induced TNF-α release, suggesting that inhibition of this kinase does not mediate the inhibitory action of luteolin. 5 In addn., DRB (a pharmacol. inhibitor of CK2) blocked TNF-α release in a concn.-dependent manner, whereas co-treatment of cells with luteolin and DRB did not have an additive effect. 6 We conclude that luteolin interferes with LPS signaling by reducing the activation of several MAPK family members and that its inhibitory action of TNF-α release correlates with inhibition of ERK, p38 and CK2 activation.
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Im, H.; Bantz, K. C.; Lee, S. H.; Johnson, T. W.; Haynes, C. L.; Oh, S.-H. Self-Assembled Plasmonic Nanoring Cavity Arrays for SERS and LSPR Biosensing Adv. Mater. 2013, 25, 2678– 2685 DOI: 10.1002/adma.201204283
[ Crossref], [ PubMed], [ CAS], Google Scholar
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Self-Assembled Plasmonic Nanoring Cavity Arrays for SERS and LSPR Biosensing
Im, Hyungsoon; Bantz, Kyle C.; Lee, Si Hoon; Johnson, Timothy W.; Haynes, Christy L.; Oh, Sang-Hyun
Advanced Materials (Weinheim, Germany) (2013), 25 (19), 2678-2685CODEN: ADVMEW; ISSN:0935-9648. (Wiley-VCH Verlag GmbH & Co. KGaA)
We have demonstrated a hybrid SERS substrate that combines the tunable LSPR of AgFON substrates with a strong field enhancement inside 10-nm metallic nanogaps. The increased LSPR sensitivity for surface-assocd. species makes the FON-gap substrate an ideal bioanal. platform to combine SERS and LSPR biosensing.
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Truong, P. L.; Kim, B. W.; Sim, S. J. Rational aspect ratio and suitable antibody coverage of gold nanorod for ultra-sensitive detection of a cancer biomarker Lab Chip 2012, 12, 1102– 1109 DOI: 10.1039/c2lc20588b
[ Crossref], [ PubMed], [ CAS], Google Scholar
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Rational aspect ratio and suitable antibody coverage of gold nanorod for ultra-sensitive detection of a cancer biomarker
Truong, Phuoc Long; Kim, Byung Woo; Sim, Sang Jun
Lab on a Chip (2012), 12 (6), 1102-1109CODEN: LCAHAM; ISSN:1473-0189. (Royal Society of Chemistry)
We report a simple, ultra-sensitive, and straightforward method for non-labeling detection of a cancer biomarker, using Rayleigh light scattering spectroscopy of the individual nanosensor based on antibody-antigen recognition and localized surface plasmon resonance (LSPR) λmax shifts. By exptl. measuring the refractive index sensitivity of Au nanorods, the Au nanorod with an aspect ratio of ∼3.5 was proven optimal for the LSPR sensing. To reduce the steric hindrance effect as well as to immobilize a large amt. of ligand on the nanoparticle surface, various mixts. contg. different molar ratios of HS(CH2)11(OCH2CH2)6OCH2COOH and HS(CH2)11(OCH2CH2)3OH were applied to form different self-assembled monolayer surfaces. The results showed that the best molar ratio for antibody conjugation was 1 : 10. When using individual Au nanorod sensors for the detection of prostate specific antigen (PSA), the lowest concn. recorded was ∼1 aM (∼6 × 105 mols.), corresponding to LSPR λmax shifts of ∼4.2 nm. These results indicate that sensor miniaturization down to the nanoscale level, the redn. of steric hindrance, and optimization of size, shape, and aspect ratio of nanorods have led to a significant improvement in the detection limit of sensors.
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Alivisatos, A. P.; Johnsson, K. P.; Peng, X. G.; Wilson, T. E.; Loweth, C. J.; Bruchez, M. P.; Schultz, P. G. Organization of ’nanocrystal molecules’ using DNA Nature 1996, 382, 609– 611 DOI: 10.1038/382609a0
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Organization of 'nanocrystal molecules' using DNA
Alivisatos, A. Paul; Johnsson, Kai P.; Peng, Xiaogang; Wilson, Troy E.; Loweth, Colin J.; Bruchez, Marcel P., Jr.; Schultz, Peter G.
Nature (London) (1996), 382 (6592), 609-611CODEN: NATUAS; ISSN:0028-0836. (Macmillan Magazines)
The authors describe a strategy for the synthesis of 'nanocrystal mols.', in which discrete nos. of Au nanocrystals are organized into spatially defined structures based on Watson-Crick base-pairing interactions. The authors attach single-stranded DNA oligonucleotides of defined length and sequence to individual nanocrystals, and these assemble into dimers and trimers on addn. of a complementary single-stranded DNA template. The authors anticipate that this approach should allow the construction of more complex two- and three-dimensional assemblies.
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Wu, B.; Chen, L. C.; Huang, Y. J.; Zhang, Y. M.; Kang, Y. J.; Kim, D. H. Multiplexed Biomolecular Detection Based on Single Nanoparticles Immobilized on Pneumatically Controlled Microfluidic Chip Plasmonics 2014, 9, 801– 807 DOI: 10.1007/s11468-013-9661-4
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Multiplexed Biomolecular Detection Based on Single Nanoparticles Immobilized on Pneumatically Controlled Microfluidic Chip
Wu, Bo; Chen, Li-Chan; Huang, Youju; Zhang, Yiming; Kang, Yuejun; Kim, Dong-Hwan
Plasmonics (2014), 9 (4), 801-807CODEN: PLASCS; ISSN:1557-1955. (Springer)
A microfluidic chip integrated with pneumatically controlled valves was developed for multiplexed biomol. detection via localized surface plasmonic resonance (LSPR) of single gold nanorod. The cost-effective microfluidic chip was assembled by polydimethylsiloxane layers and glass substrates with a precisely controlled thickness. The thin and flat microfluidic chip fitted the narrow space of dark-field microscopy and enabled the recording of single-nanoparticle LSPR responses. Aptamer-antigen-antibody sandwiched detection scheme was utilized to enhance the LSPR responses for label-free biomol. detection. This microfluidic chip successfully demonstrated the multiplexed detection of three independent analytes (PSA, IgE, and thrombin).
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Balamurugan, S.; Mayer, K. M.; Lee, S.; Soper, S. A.; Hafner, J. H.; Spivak, D. A. Nanostructure shape effects on response of plasmonic aptamer sensors J. Mol. Recognit. 2013, 26, 402– 407 DOI: 10.1002/jmr.2278
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Nanostructure shape effects on response of plasmonic aptamer sensors
Balamurugan, Subramanian; Mayer, Kathryn M.; Lee, Seunghyun; Soper, Steven A.; Hafner, Jason H.; Spivak, David A.
Journal of Molecular Recognition (2013), 26 (9), 402-407CODEN: JMORE4; ISSN:0952-3499. (Wiley-Blackwell)
A localized surface plasmon resonance (LSPR) sensor surface was fabricated by the deposition of gold nanorods on a glass substrate and subsequent immobilization of the DNA aptamer, which specifically bind to thrombin. This LSPR aptamer sensor showed a response of 6-nm λmax shift for protein binding with the detection limit of at least 10pM, indicating one of the highest sensitivities achieved for thrombin detection by optical extinction LSPR. We also tested the LSPR sensor fabricated using gold bipyramid, which showed higher refractive index sensitivity than the gold nanorods, but the overall response of gold bipyramid sensor appears to be 25% less than that of the gold nanorod substrate, despite the approx. twofold higher refractive index sensitivity. XPS anal. showed that this is due to the low surface d. of aptamers on the gold bipyramid compared with gold nanorods. The low surface d. of the aptamers on the gold bipyramid surface may be due to the effect of shape of the nanostructure on the kinetics of aptamer monolayer formation. The small size of aptamers relative to other bioreceptors is the key to achieving high sensitivity by biosensors on the basis of LSPR, demonstrated here for protein binding. The generality of aptamer sensors for protein detection using gold nanorod and gold nanobipyramid substrates is anticipated to have a large impact in the important development of sensors toward biomarkers, environmental toxins, and warfare agents. Copyright © 2013 John Wiley & Sons, Ltd.
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Bhagawati, M.; You, C. J.; Piehler, J. Quantitative Real-Time Imaging of Protein-Protein Interactions by LSPR Detection with Micropatterned Gold Nanoparticles Anal. Chem. 2013, 85, 9564– 9571 DOI: 10.1021/ac401673e
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Quantitative Real-Time Imaging of Protein-Protein Interactions by LSPR Detection with Micropatterned Gold Nanoparticles
Bhagawati, Maniraj; You, Changjiang; Piehler, Jacob
Analytical Chemistry (Washington, DC, United States) (2013), 85 (20), 9564-9571CODEN: ANCHAM; ISSN:0003-2700. (American Chemical Society)
Localized surface plasmon resonance (LSPR) offers powerful means for sensitive label-free detection of protein-protein interactions in a highly multiplexed format. The authors have here established self-assembly and surface modification of plasmonic nanostructures on solid support suitable for quant. protein-protein interaction anal. by spectroscopic and microscopic LSPR detection. These architectures were obtained by layer-by-layer assembly via electrostatic attraction. Gold nanoparticles (AuNP) were adsorbed on a biocompatible amine-terminated poly-(ethylene glycol) (PEG) polymer brush and further functionalized by poly-L-lysine graft PEG (PLL-PEG) copolymers. Stable yet reversible protein immobilization was achieved via tris-(nitrilotriacetic acid) groups incorporated into the PLL-PEG coating. Thus, site-specific immobilization of His-tagged proteins via complexed Ni(II) ions was achieved. Functional protein immobilization on the surface was confirmed by real-time detection of LSPR scattering by reflectance spectroscopy. Assocn. and dissocn. rate consts. obtained for a reversible protein-protein interaction were in good agreement with the data obtained by other surface-sensitive detection techniques. For spatially resolved detection, AuNP were assembled into micropatterns by photolithog. uncaging of surface amines. LSPR imaging of reversible protein-protein interactions was possible in a conventional wide field microscope, yielding detection limits of ∼30 protein mols. within a diffraction-limited surface area.
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Cohavi, O.; Reichmann, D.; Abramovich, R.; Tesler, A. B.; Bellapadrona, G.; Kokh, D. B.; Wade, R. C.; Vaskevich, A.; Rubinstein, I.; Schreiber, G. A Quantitative, Real-Time Assessment of Binding of Peptides and Proteins to Gold Surfaces Chem. - Eur. J. 2011, 17, 1327– 1336 DOI: 10.1002/chem.201001781
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A Quantitative, Real-Time Assessment of Binding of Peptides and Proteins to Gold Surfaces
Cohavi, Ori; Reichmann, Dana; Abramovich, Renne; Tesler, Alexander B.; Bellapadrona, Giuliano; Kokh, Daria B.; Wade, Rebecca C.; Vaskevich, Alexander; Rubinstein, Israel; Schreiber, Gideon
Chemistry - A European Journal (2011), 17 (4), 1327-1336, S1327/1-S1327/7CODEN: CEUJED; ISSN:0947-6539. (Wiley-VCH Verlag GmbH & Co. KGaA)
Interactions of peptides and proteins with inorg. surfaces are important to both natural and artificial systems; however, a detailed understanding of such interactions is lacking. In this study, we applied new approaches to quant. measure the binding of amino acids and proteins to gold surfaces. Real-time surface plasmon resonance (SPR) measurements showed that TEM1-β-lactamase inhibitor protein (BLIP) interacts only weakly with Au nanoparticles (NPs). However, fusion of three histidine residues to BLIP (3H-BLIP) resulted in a significant increase in the binding to the Au NPs, which further increased when the histidine tail was extended to six histidines (6H-BLIP). Further increasing the no. of His residues had no effect on the binding. A parallel study using continuous (111)-textured Au surfaces and single-cryst., (111)-oriented, Au islands by ellipsometry, FTIR, and localized surface plasmon resonance (LSPR) spectroscopy further confirmed the results, validating the broad applicability of Au NPs as model surfaces. Evaluating the binding of all other natural amino acid homotripeptides fused to BLIP (except Cys and Pro) showed that arom. and pos.-charged residues bind preferentially to Au with respect to small aliph. and neg. charged residues, and that the rate of assocn. is related to the potency of binding. The binding of all fusions was irreversible. These findings were substantiated by SPR measurements of synthesized, free, sol. tripeptides using Au-NP-modified SPR chips. Here, however, the binding was reversible allowing for detn. of binding affinities that correlate with the binding potencies of the related BLIP fusions. Competition assays performed between 3H-BLIP and the histidine tripeptide (3 His) suggest that Au binding residues promote the adsorption of proteins on the surface, and by this facilitate the irreversible interaction of the polypeptide chain with Au. The binding of amino acids to Au was simulated by using a continuum solvent model, showing agreement with the exptl. values. These results, together with the obsd. binding potencies and kinetics of the BLIP fusions and free peptides, suggest a binding mechanism that is markedly different from biol. protein-protein interactions.
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Chen, S.; Svedendahl, M.; Van Duyne, R. P.; Kall, M. Plasmon-Enhanced Colorimetric ELISA with Single Molecule Sensitivity Nano Lett. 2011, 11, 1826– 1830 DOI: 10.1021/nl2006092
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Plasmon-Enhanced Colorimetric ELISA with Single Molecule Sensitivity
Chen, Si; Svedendahl, Mikael; Van Duyne, Richard P.; Kaell, Mikael
Nano Letters (2011), 11 (4), 1826-1830CODEN: NALEFD; ISSN:1530-6984. (American Chemical Society)
Robust but ultrasensitive biosensors with a capability of detecting low abundance biomarkers could revolutionize clin. diagnostics and enable early detection of cancer, neurol. diseases, and infections. The authors utilized a combination of localized surface plasmon resonance (LSPR) refractive index sensing and the well-known ELISA to develop a simple colorimetric biosensing methodol. with single mol. sensitivity. The technique is based on spectral imaging of a large no. of isolated gold nanoparticles. Each particle binds a variable no. of horseradish peroxidase (HRP) enzyme mols. that catalyze a localized pptn. reaction at the particle surface. The enzymic reaction dramatically amplifies the shift of the LSPR scattering max., λmax, and makes it possible to detect the presence of only one or a few HRP mols. per particle.
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Zhang, J.; Wang, L.; Pan, D.; Song, S.; Boey, F. Y. C.; Zhang, H.; Fan, C. Visual cocaine detection with gold nanoparticles and rationally engineered aptamer structures Small 2008, 4, 1196– 1200 DOI: 10.1002/smll.200800057
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Visual cocaine detection with gold nanoparticles and rationally engineered aptamer structures
Zhang, Juan; Wang, Lihua; Pan, Dun; Song, Shiping; Boey, Freddy Y. C.; Zhang, Hua; Fan, Chunhai
Small (2008), 4 (8), 1196-1200CODEN: SMALBC; ISSN:1613-6810. (Wiley-VCH Verlag GmbH & Co. KGaA)
A bioassay strategy is designed to detect small-mol. targets such as cocaine, potassium, and adenosine, based on gold nanoparticles and engineered DNA aptamers. In this design, an aptamer is engineered to be two pieces of random, coil-like single-stranded DNA, which reassembles into the intact aptamer tertiary structure in the presence of the specific target. Au nanoparticles can effectively differentiate between these two states via their characteristic surface-plasmon resonance-based color change. Using this method, cocaine in the low-micromolar range is selectively detected within minutes. This strategy is also generic and applicable to the detection of several other small-mol. targets.
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Guerreiro, J. R. L.; Frederiksen, M.; Bochenkov, V. E.; De Freitas, V.; Ferreira Sales, M. G.; Sutherland, D. S. Multifunctional Biosensor Based on Localized Surface Plasmon Resonance for Monitoring Small Molecule-Protein Interaction ACS Nano 2014, 8, 7958– 7967 DOI: 10.1021/nn501962y
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Multifunctional Biosensor Based on Localized Surface Plasmon Resonance for Monitoring Small Molecule-Protein Interaction
Guerreiro, Joana Rafaela Lara; Frederiksen, Maj; Bochenkov, Vladimir E.; De Freitas, Victor; Ferreira Sales, Maria Goreti; Sutherland, Duncan Steward
ACS Nano (2014), 8 (8), 7958-7967CODEN: ANCAC3; ISSN:1936-0851. (American Chemical Society)
We report an optical sensor based on localized surface plasmon resonance (LSPR) to study small-mol. protein interaction combining high sensitivity refractive index sensing for quant. binding information and subsequent conformation-sensitive plasmon-activated CD spectroscopy. The interaction of α-amylase and a small-size mol. (PGG, pentagalloyl glucose) was log concn.-dependent from 0.5 to 154 μM. In situ tests were addnl. successfully applied to the anal. of real wine samples. These studies demonstrate that LSPR sensors to monitor small mol.-protein interactions in real time and in situ, which is a great advance within technol. platforms for drug discovery.
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Chianella, I.; Guerreiro, A.; Moczko, E.; Caygill, J. S.; Piletska, E. V.; De Vargas Sansalvador, I. M.; Whitcombe, M. J.; Piletsky, S. A. Direct Replacement of Antibodies with Molecularly Imprinted Polymer Nanoparticles in ELISA-Development of a Novel Assay for Vancomycin Anal. Chem. 2013, 85, 8462– 8468 DOI: 10.1021/ac402102j
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Direct Replacement of Antibodies with Molecularly Imprinted Polymer Nanoparticles in ELISA-Development of a Novel Assay for Vancomycin
Chianella, Iva; Guerreiro, Antonio; Moczko, Ewa; Caygill, J. Sarah; Piletska, Elena V.; De Vargas Sansalvador, Isabel M. Perez; Whitcombe, Michael J.; Piletsky, Sergey A.
Analytical Chemistry (Washington, DC, United States) (2013), 85 (17), 8462-8468CODEN: ANCHAM; ISSN:0003-2700. (American Chemical Society)
A simple and straightforward technique for coating microplate wells with molecularly imprinted polymer nanoparticles (nanoMIPs) to develop assays similar to the ELISA is presented here for the first time. NanoMIPs were synthesized by a solid-phase approach with an immobilized vancomycin (template) and characterized using Biacore 3000, dynamic light scattering, and electron microscopy. Immobilization, blocking, and washing conditions were optimized in microplate format. The detection of vancomycin was achieved in competitive binding expts. with a horseradish peroxidase-vancomycin conjugate. The assay was capable of measuring vancomycin in buffer and in blood plasma within the range of 0.001-70 nM with a detection limit of 0.0025 nM (2.5 pM). The sensitivity of the assay was 3 orders of magnitude better than a previously described ELISA based on antibodies. In these expts., nanoMIPs showed high affinity and minimal interference from blood plasma components. Immobilized nanoMIPs were stored for 1 mo at room temp. without any detrimental effects to their binding properties. The high affinity of nanoMIPs and the lack of a requirement for cold chain logistics make them an attractive alternative to traditional antibodies used in ELISA.
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Abbas, A.; Tian, L. M.; Morrissey, J. J.; Kharasch, E. D.; Singamaneni, S. Hot Spot-Localized Artificial Antibodies for Label-Free Plasmonic Biosensing Adv. Funct. Mater. 2013, 23, 1789– 1797 DOI: 10.1002/adfm.201202370
[ Crossref], [ PubMed], [ CAS], Google Scholar
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Hot Spot-Localized Artificial Antibodies for Label-Free Plasmonic Biosensing
Abbas, Abdennour; Tian, Limei; Morrissey, Jeremiah J.; Kharasch, Evan D.; Singamaneni, Srikanth
Advanced Functional Materials (2013), 23 (14), 1789-1797CODEN: AFMDC6; ISSN:1616-301X. (Wiley-VCH Verlag GmbH & Co. KGaA)
The development of biomol. imprinting over the last decade has raised promising perspectives in replacing natural antibodies with artificial antibodies. A significant no. of reports have been dedicated to imprinting of org. and inorg. nanostructures, but very few were performed on nanomaterials with a transduction function. Herein, a relatively fast and efficient plasmonic hot spot-localized surface imprinting of gold nanorods using reversible template immobilization and siloxane copolymn. is described. The technique enables a fine control of the imprinting process at the nanometer scale and provides a nanobiosensor with high selectivity and reusability. Proof of concept was established by the detection of neutrophil gelatinase-assocd. lipocalin (NGAL), a biomarker for acute kidney injury, using localized surface plasmon resonance spectroscopy. The work represents a valuable step towards plasmonic nanobiosensors with synthetic antibodies for label-free and cost-efficient diagnostic assays. It is expected that this novel class of surface imprinted plasmonic nanomaterials will open up new possibilities in advancing biomedical applications of plasmonic nanostructures.
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Hole-mask colloidal lithography
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Advanced Materials (Weinheim, Germany) (2007), 19 (23), 4297-4302CODEN: ADVMEW; ISSN:0935-9648. (Wiley-VCH Verlag GmbH & Co. KGaA)
Hole-mask colloidal lithog. represents a truly versatile and simple bottom-up nanofabrication method based on colloidal self-assembly lithog. patterning. The technique provides an effective means of patterning vast surface areas with diverse functional nanoarchitectures. Examples include arrays of nanodisks, oriented elliptical nanostructures, (binary) nanodisk pairs, nanocones on extended surfaces and nanodisks embedded in a surrounding matrix.
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A review. The detection of specific proteins as biomarkers of disease, health status, environmental monitoring, food quality, control of fermenters and civil defense purposes means that biosensors for these targets will become increasingly more important. Among the technologies used for building specific recognition properties, molecularly imprinted polymers (MIPs) are attracting much attention. In this crit. review we describe many methods used for imprinting recognition for protein targets in polymers and their incorporation with a no. of transducer platforms with the aim of identifying the most promising approaches for the prepn. of MIP-based protein sensors (277 refs.).
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Biosensors & Bioelectronics (2013), 45 (), 237-244CODEN: BBIOE4; ISSN:0956-5663. (Elsevier B.V.)
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ACS Photonics (2015), 2 (2), 256-262CODEN: APCHD5; ISSN:2330-4022. (American Chemical Society)
We evaluate and compare the sensitivity of gold nanodisks on silica substrates and nanoholes made in silica-supported gold films, two of the most common sensor structures used in plasmonic biosensing. An alumina overcoat was applied by at. layer deposition (ALD) to precisely control the interfacial refractive index and det. the evanescent plasmonic field decay length. The results are in good agreement with anal. models and biomol. binding expts. for the two substrates. We found that nanodisks outperform nanoholes for thin dielec. coatings (<∼20 nm), while the opposite holds true for thicker coatings (>∼20 nm). The optimum nanoplasmonic transducer element for a given biorecognition reaction can be chosen based on exptl. detd. bulk sensitivities/noise levels and theor. estd. evanescent field decay lengths.
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Films formed from saliva on surfaces are important for the maintenance of oral health and integrity by protection against chem. and/or biol. agents. The aim of the present study was to investigate adsorbed amts., thickness, and structure of films formed from human whole saliva on alumina surfaces by means of in situ ellipsometry, neutron reflectivity, and at. force microscopy. Alumina (Al2O3, synthetic sapphire) is a relevant and interesting substrate for saliva adsorption studies as it has an isoelec. point close to that of tooth enamel. The results showed that saliva adsorbs rapidly on alumina. The film could be modeled in two layers: an inner and dense thin region that forms a uniform layer and an outer, more diffuse and thicker region that protrudes toward the bulk of the soln. The film morphol. described a uniformly covering dense layer and a second outer layer contg. polydisperse adsorbed macromols. or aggregates.
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A comparative study of protein adsorption on titanium oxide surfaces using in situ ellipsometry, optical waveguide lightmode spectroscopy, and quartz crystal microbalance/dissipation
Hook, F.; Voros, J.; Rodahl, M.; Kurrat, R.; Boni, P.; Ramsden, J. J.; Textor, M.; Spencer, N. D.; Tengvall, P.; Gold, J.; Kasemo, B.
Colloids and Surfaces, B: Biointerfaces (2002), 24 (2), 155-170CODEN: CSBBEQ; ISSN:0927-7765. (Elsevier Science B.V.)
The adsorption kinetics of three model proteins--human serum albumin, fibrinogen and Hb--has been measured and compared using three different exptl. techniques: optical waveguide lightmode spectroscopy (OWLS), ellipsometry (ELM) and quartz crystal microbalance (QCM-D). The studies were complemented by also monitoring the corresponding antibody interactions with the pre-adsorbed protein layer. All measurements were performed with identically prepd. titanium oxide coated substrates. All three techniques are suitable to follow in-situ kinetics of protein-surface and protein-antibody interactions, and provide quant. values of the adsorbed adlayer mass. The results have, however, different phys. contents. The optical techniques OWLS and ELM provide in most cases consistent and comparable results, which can be straightforwardly converted to adsorbed protein molar ('dry') mass. QCM-D, produces measured values that are generally higher in terms of mass. This, in turn, provides valuable, complementary information in two respects: (i) the mass calcd. from the resonance frequency shift includes both protein mass and water that binds or hydrodynamically couples to the protein adlayer; and (ii) anal. of the energy dissipation in the adlayer and its magnitude in relation to the frequency shift (c.f. adsorbed mass) provides insight about the mech./structural properties such as viscoelasticity.
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Abstract
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Figure 1
Figure 1. Schematic representation of MIP-Au nanodisks surface imprinting followed by LSPR detection of small molecules. (A) Bare Au nanodisks. (B) Thiophenecarboxylic acid thiol added to Au nanodisks. (C) AMY or saliva adsorption. (D) Free radical polymerization of MIP. (E) Enzymatic protein removal, proteinase K. (F) AMY or saliva incubation. (G) Polyphenol interaction with protein on the surface.
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Figure 2
Figure 2. LSPR spectral response for the molecular imprinting process (MIP). (A) AMY imprinting, (B) saliva imprinting, and (C) nonimprinted polymer (NIP). Blue line corresponds to bare Au nanodisks (square), red line to AMY 10 μM or saliva adsorption (inverted square), green line to polymer polymerization (circles), and purple line to protein removal (triangle).
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Figure 3
Figure 3. AFM images in liquid of (a) Au nanodisks (control), (b) nonimprinted material, and (c) amylase imprinted on Au nanodisks substrate.
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Figure 4
Figure 4. Experimental (A) and FDTD simulated (B) extinction spectra of Au nanodisks substrates immersed in different refractive index solutions. Correlation peak position vs refractive index units through FDTD for 7 nm (C) and 14 nm (D) layer thickness. (E) Field enhancement (E² scale 0–150) distribution image of the Au nanodisks. (F) Two-dimensional cross section field map.
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Figure 5
Figure 5. Ratio of polyphenols mass/protein mass for (A) PGG, (B) B3, and (C) catechin. AMY (triangles) and saliva (circles).
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References
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  Nature (London, United Kingdom) (2001), 414 (6866), 863-864CODEN: NATUAS; ISSN:0028-0836. (Nature Publishing Group)
  Ethanol-free exts. from 23 red wines, four white wines, one rose wine and one red grape juice were prepd. to det. their inhibitory effect on the synthesis of endothelin-1 (ET-1), a vasoactive peptide that is crucial in the development of coronary atherosclerosis. The degree of inhibition of ET-1 by red wine was correlated with its total phenol content. The red-grape juice did not significantly inhibit ET-1 synthesis, while no effect was obsd. with white and rose wine. The polyphenol content of the red wines were responsible for their inhibitory effect on ET-1 synthesis. The red wine ext. caused a significant change in the cell morphol. and a redistribution of phosphotyrosine staining. These effects on tyrosine phosphorylation were due to the modified tyrosine-kinase signaling in endothelial cells. Thus, moderate intake of red wine can prevent coronary heart disease.
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6. 6
  Fito, M.; Cladellas, M.; de la Torre, R.; Marti, J.; Munoz, D.; Schroder, H.; Alcantara, M.; Pujadas-Bastardes, M.; Marrugat, J.; Lopez-Sabater, M. C.; Bruguera, J.; Covas, M. I. Anti-inflammatory effect of virgin olive oil in stable coronary disease patients: a randomized, crossover, controlled trial Eur. J. Clin. Nutr. 2008, 62, 570– 574 DOI: 10.1038/sj.ejcn.1602724
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  Anti-inflammatory effect of virgin olive oil in stable coronary disease patients: a randomized, crossover, controlled trial
  Fito, M.; Cladellas, M.; de la Torre, R.; Marti, J.; Munoz, D.; Schroeder, H.; Alcantara, M.; Pujadas-Bastardes, M.; Marrugat, J.; Lopez-Sabater, M. C.; Bruguera, J.; Covas, M. I.
  European Journal of Clinical Nutrition (2008), 62 (4), 570-574CODEN: EJCNEQ; ISSN:0954-3007. (Nature Publishing Group)
  Objectives: To assess the effect of two similar olive oils, but with differences in their phenolic compds. (powerful antioxidant compds.), on inflammatory markers in stable coronary heart disease patients. Design: Placebo-controlled, crossover, randomized trial. Setting: Cardiol. Department of Hospital del Mar and Institut Municipal d'Investigacio Medica (Barcelona). Subjects: Twenty-eight stable coronary heart disease patients. Interventions: A raw daily dose of 50 mL of virgin and refined olive oil (ROO) was sequentially administered over two periods of 3-wk, preceded by 2-wk washout periods in which ROO was used. Results: Interleukin-6 (P<0.002) and C-reactive protein (P=0.024) decreased after virgin olive oil intervention. No changes were obsd. in sol. intercellular and vascular adhesion mols., glucose and lipid profile. Conclusions: Consumption of virgin olive oil, could provide beneficial effects in stable coronary heart disease patients as an addnl. intervention to the pharmacol. treatment.
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7. 7
  Gescher, A.; Pastorino, U.; Plummer, S. M.; Manson, M. M. Suppression of tumour development by substances derived from the diet - mechanisms and clinical implications Br. J. Clin. Pharmacol. 1998, 45, 1– 12 DOI: 10.1046/j.1365-2125.1998.00640.x
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  Suppression of tumor development by substances derived from the diet - mechanisms and clinical implications
  Gescher, Andreas; Pastorino, Ugo; Plummer, Simon M.; Manson, Margaret M.
  British Journal of Clinical Pharmacology (1998), 45 (1), 1-12CODEN: BCPHBM; ISSN:0306-5251. (Blackwell Science Ltd.)
  A review with 99 refs. The concept that cancer can be prevented, or its onset postponed, by certain diet-derived substances is eliciting considerable interest. Agents which interfere with tumor promotion and progression are of potential clin. value. As chemopreventive agents have to be administered over a long period of time to establish whether they possess efficacy in humans, it is important to establish their lack of toxicity. The desire to select the best drug candidates for clin. trials and the necessity to monitor efficacy in the short and intermediate terms give the identification of specific mechanism-based in vivo markers of biol. activity a high priority. Antioxidn., inhibition of arachidonic acid metab., modulation of cellular signal transduction pathways, inhibition of hormone and growth factor activity, and inhibition of oncogene activity are discussed as mechanisms by which the soybean constituent genistein, the curry ingredient curcumin, and the vitamin A analog 13-cis-retinoic acid exert their tumor suppression activity. Better understanding of the mechanisms will help to screen and discover new chemopreventive agents and to identify surrogate markers to assess the outcome of clin. chemoprevention trials.
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8. 8
  Middleton, E.; Kandaswami, C.; Theoharides, T. C. The effects of plant flavonoids on mammalian cells: Implications for inflammation, heart disease, and cancer Pharmacol. Rev. 2000, 52, 673– 751
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  The effects of plant flavonoids on mammalian cells: Implications for inflammation, heart disease, and cancer
  Middleton, Elliott, Jr.; Kandaswami, Chithan; Theoharides, Theoharis C.
  Pharmacological Reviews (2000), 52 (4), 673-751CODEN: PAREAQ; ISSN:0031-6997. (American Society for Pharmacology and Experimental Therapeutics)
  A review with about 1000 refs. Flavonoids are nearly ubiquitous in plants and are recognized as the pigments responsible for the colors of leaves, esp. in autumn. They are rich in seeds, citrus fruits, olive oil, tea, and red wine. They are low mol. wt. compds. composed of a three-ring structure with various substitutions. This basic structure is shared by tocopherols (vitamin E). Flavonoids can be subdivided according to the presence of an oxy group at position 4, a double bond between carbon atoms 2 and 3, or a hydroxyl group in position 3 of the C (middle) ring. These characteristics appear to also be required for best activity, esp. antioxidant and antiproliferative, in the systems studied. The particular hydroxylation pattern of the B ring of the flavonoles increases their activities, esp. in inhibition of mast cell secretion. Certain plants and spices contg. flavonoids have been used for thousands of years in traditional Eastern medicine. In spite of the voluminous literature available, however, Western medicine has not yet used flavonoids therapeutically, even though their safety record is exceptional. Suggestions are made where such possibilities may be worth pursuing.
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9. 9
  Aggarwal, B. B.; Shishodia, S. Molecular targets of dietary agents for prevention and therapy of cancer Biochem. Pharmacol. 2006, 71, 1397– 1421 DOI: 10.1016/j.bcp.2006.02.009
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  Molecular targets of dietary agents for prevention and therapy of cancer
  Aggarwal, Bharat B.; Shishodia, Shishir
  Biochemical Pharmacology (2006), 71 (10), 1397-1421CODEN: BCPCA6; ISSN:0006-2952. (Elsevier B.V.)
  A review. While fruits and vegetables are recommended for prevention of cancer and other diseases, their active ingredients (at the mol. level) and their mechanisms of action less well understood. Extensive research during the last half century has identified various mol. targets that can potentially be used not only for the prevention of cancer but also for treatment. However, lack of success with targeted monotherapy resulting from bypass mechanisms has forced researchers to employ either combination therapy or agents that interfere with multiple cell-signaling pathways. In this review, we present evidence that numerous agents identified from fruits and vegetables can interfere with several cell-signaling pathways. The agents include curcumin (turmeric), resveratrol (red grapes, peanuts, and berries), genistein (soybean), diallyl sulfide (allium), S-allyl cysteine (allium), allicin (garlic), lycopene (tomato), capsaicin (red chilli), diosgenin (fenugreek), 6-gingerol (ginger), ellagic acid (pomegranate), ursolic acid (apples, pears, prunes), silymarin (milk thistle), anethol (anise, camphor, and fennel), catechins (green tea), eugenol (cloves), indole-3-carbinol (cruciferous vegetables), limonene (citrus fruits), β-carotene (carrots), and dietary fiber. For instance, the cell-signaling pathways inhibited by curcumin alone include NF-κB, AP-1, STAT3, Akt, Bcl-2, Bcl-XL, caspases, PARP, IKK, EGFR, HER2, JNK, MAPK, COX2, and 5-LOX. The active principle identified in fruit and vegetables and the mol. targets modulated may be the basis for how these dietary agents not only prevent but also treat cancer and other diseases. This work reaffirms what Hippocrates said 25 centuries ago, let food be thy medicine and medicine be thy food.
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10. 10
  Daglia, M. Polyphenols as antimicrobial agents Curr. Opin. Biotechnol. 2012, 23, 174– 181 DOI: 10.1016/j.copbio.2011.08.007
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  Polyphenols as antimicrobial agents
  Daglia, Maria
  Current Opinion in Biotechnology (2012), 23 (2), 174-181CODEN: CUOBE3; ISSN:0958-1669. (Elsevier B.V.)
  A review. Polyphenols are secondary metabolites produced by higher plants, which play multiple essential roles in plant physiol. and have potential healthy properties on human organism, mainly as antioxidants, anti-allergic, anti-inflammatory, anticancer, antihypertensive, and antimicrobial agents. In the present review the antibacterial, antiviral, and antifungal activities of the most active polyphenol classes are reported, highlighting, where investigated, the mechanisms of action and the structure-activity relationship. Moreover, considering that the microbial resistance has become an increasing global problem, and there is a compulsory need to find out new potent antimicrobial agents as accessories to antibiotic therapy, the synergistic effect of polyphenols in combination with conventional antimicrobial agents against clin. multidrug-resistant microorganisms is discussed.
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11. 11
  Ferrazzano, G. F.; Amato, I.; Ingenito, A.; Zarrelli, A.; Pinto, G.; Pollio, A. Plant Polyphenols and Their Anti-Cariogenic Properties: A Review Molecules 2011, 16, 1486– 1507 DOI: 10.3390/molecules16021486
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  Plant polyphenols and their anti-cariogenic properties: a review
  Ferrazzano, Gianmaria F.; Amato, Ivana; Ingenito, Aniello; Zarrelli, Armando; Pinto, Gabriele; Pollio, Antonino
  Molecules (2011), 16 (), 1486-1507CODEN: MOLEFW; ISSN:1420-3049. (MDPI AG)
  A review. Polyphenols constitute one of the most common groups of substances in plants. Polyphenolic compds. have been reported to have a wide range of biol. activities, many of which are related to their conventional antioxidant action; however, increasing scientific knowledge has highlighted their potential activity in preventing oral disease, including the prevention of tooth decay. The aim of this review is to show the emerging findings on the anti-cariogenic properties of polyphenols, which have been obtained from several in vitro studies investigating the effects of these bioactive mols. against Streptococcus mutans, as well as in vivo studies. The anal. of the literature supports the anti-bacterial role of polyphenols on cariogenic streptococci, suggesting (1) a direct effect against S. mutans; (2) an interaction with microbial membrane proteins inhibiting the adherence of bacterial cells to the tooth surface; and (3) the inhibition of glucosyl transferase and amylase. However, more studies, particularly in vivo and in situ, are necessary to establish conclusive evidence for the effectiveness and the clin. applications of these compds. in the prevention of dental caries. It is essential to better det. the nature and distribution of these compds. in our diet and to identify which of the hundreds of existing polyphenols are likely to provide the greatest effects.
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12. 12
  Link, A.; Balaguer, F.; Goel, A. Cancer chemoprevention by dietary polyphenols: Promising role for epigenetics Biochem. Pharmacol. 2010, 80, 1771– 1792 DOI: 10.1016/j.bcp.2010.06.036
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  Cancer chemoprevention by dietary polyphenols: Promising role for epigenetics
  Link, Alexander; Balaguer, Francesc; Goel, Ajay
  Biochemical Pharmacology (2010), 80 (12), 1771-1792CODEN: BCPCA6; ISSN:0006-2952. (Elsevier B.V.)
  A review. Epigenetics refers to heritable changes that are not encoded in the DNA sequence itself, but play an important role in the control of gene expression. In mammals, epigenetic mechanisms include changes in DNA methylation, histone modifications and non-coding RNAs. Although epigenetic changes are heritable in somatic cells, these modifications are also potentially reversible, which makes them attractive and promising avenues for tailoring cancer preventive and therapeutic strategies. Burgeoning evidence in the last decade has provided unprecedented clues that diet and environmental factors directly influence epigenetic mechanisms in humans. Dietary polyphenols from green tea, turmeric, soybeans, broccoli and others have shown to possess multiple cell-regulatory activities within cancer cells. More recently, we have begun to understand that some of the dietary polyphenols may exert their chemopreventive effects in part by modulating various components of the epigenetic machinery in humans. In this article, the authors 1st discuss the contribution of diet and environmental factors on epigenetic alterations; subsequently, the authors provide a comprehensive review of literature on the role of various dietary polyphenols. In particular, we summarize the current knowledge on a large no. of dietary agents and their effects on DNA methylation, histone modifications and regulation of expression of the non-coding miRNAs in various in vitro and in vivo models. We emphasize how increased understanding of the chemopreventive effects of dietary polyphenols on specific epigenetic alterations may provide unique and yet unexplored novel and highly effective chemopreventive strategies for reducing the health burden of cancer and other diseases in humans.
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13. 13
  Izzotti, A.; Cartiglia, C.; Steele, V. E.; De Flora, S. MicroRNAs as targets for dietary and pharmacological inhibitors of mutagenesis and carcinogenesis Mutat. Res., Rev. Mutat. Res. 2012, 751, 287– 303 DOI: 10.1016/j.mrrev.2012.05.004
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  MicroRNAs as targets for dietary and pharmacological inhibitors of mutagenesis and carcinogenesis
  Izzotti, Alberto; Cartiglia, Cristina; Steele, Vernon E.; De Flora, Silvio
  Mutation Research, Reviews in Mutation Research (2012), 751 (2), 287-303CODEN: MRRRFK; ISSN:1383-5742. (Elsevier B.V.)
  A review. MicroRNAs (miRNAs) have been implicated in many biol. processes, cancer, and other diseases. In addn., miRNAs are dysregulated following exposure to toxic and genotoxic agents. Here we review studies evaluating modulation of miRNAs by dietary and pharmacol. agents, which could potentially be exploited for inhibition of mutagenesis and carcinogenesis. This review covers natural agents, including vitamins, oligoelements, polyphenols, isoflavones, indoles, isothiocyanates, phospholipids, saponins, anthraquinones and polyunsatd. fatty acids, and synthetic agents, including thiols, nuclear receptor agonists, histone deacetylase inhibitors, antiinflammatory drugs, and selective estrogen receptor modulators. As many as 145 miRNAs, involved in the control of a variety of carcinogenesis mechanisms, were modulated by these agents, either individually or in combination. Most studies used cancer cells in vitro with the goal of modifying their phenotype by changing miRNA expression profiles. In vivo studies evaluated regulation of miRNAs by chemopreventive agents in organs of mice and rats, either untreated or exposed to carcinogens, with the objective of evaluating their safety and efficacy. The tissue specificity of miRNAs could be exploited for the chemoprevention of site-specific cancers, and the study of polymorphic miRNAs is expected to predict the individual response to chemopreventive agents as a tool for developing new prevention strategies.
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14. 14
  Li, Y. Y.; Zhang, T. Targeting cancer stem cells by curcumin and clinical applications Cancer Lett. 2014, 346, 197– 205 DOI: 10.1016/j.canlet.2014.01.012
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  Targeting cancer stem cells by curcumin and clinical applications
  Li, Yanyan; Zhang, Tao
  Cancer Letters (New York, NY, United States) (2014), 346 (2), 197-205CODEN: CALEDQ; ISSN:0304-3835. (Elsevier)
  A review. Curcumin is a well-known dietary polyphenol derived from the rhizomes of turmeric, an Indian spice. The anticancer effect of curcumin has been demonstrated in many cell and animal studies, and recent research has shown that curcumin can target cancer stem cells (CSCs). CSCs are proposed to be responsible for initiating and maintaining cancer, and contribute to recurrence and drug resistance. A no. of studies have suggested that curcumin has the potential to target CSCs through regulation of CSC self-renewal pathways (Wnt/β-catenin, Notch, sonic hedgehog) and specific microRNAs involved in acquisition of epithelial-mesenchymal transition (EMT). The potential impact of curcumin, alone or in combination with other anticancer agents, on CSCs was evaluated as well. Furthermore, the safety and tolerability of curcumin have been well-established by numerous clin. studies. Importantly, the low bioavailability of curcumin has been dramatically improved through the use of structural analogs or special formulations. More clin. trials are underway to investigate the efficacy of this promising agent in cancer chemoprevention and therapy. In this article, we review the effects of curcumin on CSC self-renewal pathways and specific microRNAs, as well as its safety and efficacy in recent human studies. In conclusion, curcumin could be a very promising adjunct to traditional cancer treatments.
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15. 15
  Santangelo, C.; Vari, R.; Scazzocchio, B.; Di Benedetto, R.; Filesi, C.; Masella, R. Polyphenols, intracellular signalling and inflammation Ann. Ist. Super. Sanita 2007, 43, 394– 405
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  Polyphenols, intracellular signalling and inflammation
  Santangelo, Carmela; Vari, Rosaria; Scazzocchio, Beatrice; Di Benedetto, Roberta; Filesi, Carmela; Masella, Roberta
  Annali dell'Istituto Superiore di Sanita (2007), 43 (4), 394-405CODEN: AISSAW; ISSN:0021-2571. (Istituto Superiore di Sanita)
  A review. Excessive inflammation is considered as a crit. factor in many human diseases, including cancer, obesity, type II diabetes, cardiovascular diseases, neurodegenerative diseases and aging. Compds. derived from botanic sources, such as phenolic compds., have shown anti-inflammatory activity in vitro and in vivo. Recent data suggest that polyphenols can work as modifiers of signal transduction pathways to elicit their beneficial effects. These natural compds. express anti-inflammatory activity by modulation of pro-inflammatory gene expression such as cyclooxygenase, lipoxygenase, nitric oxide synthases and several pivotal cytokines, mainly by acting through nuclear factor-kappa B and mitogen-activated protein kinase signalling. This review will discuss recent data on the control of inflammatory signalling exerted by some dietary polyphenols contained in Mediterranean diet. A clear understanding of the mol. mechanisms of action of phenolic compds. is crucial in the valuation of these potent mols. as potential prophylactic and therapeutic agents.
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16. 16
  Albini, A.; Tosetti, F.; Li, V. W.; Noonan, D. M.; Li, W. W. Cancer prevention by targeting angiogenesis Nat. Rev. Clin. Oncol. 2012, 9, 498– 509 DOI: 10.1038/nrclinonc.2012.120
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  Cancer prevention by targeting angiogenesis
  Albini, Adriana; Tosetti, Francesca; Li, Vincent W.; Noonan, Douglas M.; Li, William W.
  Nature Reviews Clinical Oncology (2012), 9 (9), 498-509CODEN: NRCOAA; ISSN:1759-4774. (Nature Publishing Group)
  A review. Healthy individuals can harbor microscopic tumors and dysplastic foci in different organs in an undetectable and asymptomatic state for many years. These lesions do not progress in the absence of angiogenesis or inflammation. Targeting both processes before clin. manifestation can prevent tumor growth and progression. Angioprevention is a chemoprevention approach that interrupts the formation of new blood vessels when tumor cell foci are in an indolent state. Many efficacious chemopreventive drugs function by preventing angiogenesis in the tumor microenvironment. Blocking the vascularization of incipient tumors should maintain a dormancy state such that neoplasia or cancer exist without disease. The current limitations of antiangiogenic cancer therapy may well be related to the use of antiangiogenic agents too late in the disease course. In this Review, we suggest mechanisms and strategies for using antiangiogenesis agents in a safe, preventive clin. angioprevention setting, proposing different levels of clin. angioprevention according to risk, and indicate potential drugs to be employed at these levels. Finally, angioprevention may go well beyond cancer in the prevention of a range of chronic disorders where angiogenesis is crucial, including different forms of inflammatory or autoimmune diseases, ocular disorders, and neurodegeneration.
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17. 17
  Potapovich, A. I.; Lulli, D.; Fidanza, P.; Kostyuk, V. A.; De Luca, C.; Pastore, S.; Korkina, L. G. Plant polyphenols differentially modulate inflammatory responses of human keratinocytes by interfering with activation of transcription factors NF kappa B and AhR and EGFR-ERK pathway Toxicol. Appl. Pharmacol. 2011, 255, 138– 149 DOI: 10.1016/j.taap.2011.06.007
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  Plant polyphenols differentially modulate inflammatory responses of human keratinocytes by interfering with activation of transcription factors NFκB and AhR and EGFR-ERK pathway
  Potapovich, Alla I.; Lulli, Daniela; Fidanza, Paolo; Kostyuk, Vladimir A.; De Luca, Chiara; Pastore, Saveria; Korkina, Liudmila G.
  Toxicology and Applied Pharmacology (2011), 255 (2), 138-149CODEN: TXAPA9; ISSN:0041-008X. (Elsevier B.V.)
  Mol. mechanisms underlying modulation of inflammatory responses in primary human keratinocytes by plant polyphenols (PPs), namely the glycosylated phenylpropanoid verbascoside, the stilbenoid resveratrol and its glycoside polydatin, and the flavonoid quercetin and its glycoside rutin were evaluated. As non-lethal stimuli, the prototypic ligand for epidermal growth factor receptor (EGFR) transforming growth factor alpha (TGFalpha), the combination of tumor necrosis factor (TNFalpha) and interferon (IFNgamma) (T/I), UVA + UVB irradn., and bacterial lipopolysaccharide (LPS) were used. We demonstrated differential modulation of inflammatory responses in keratinocytes at signal transduction, gene transcription, and protein synthesis levels as a function of PP chem. structure, the pro-inflammatory trigger used, and PP interaction with intracellular detoxifying systems. The PPs remarkably inhibited constitutive, LPS- and T/I-induced but not TGFalpha-induced ERK phosphorylation. They also suppressed NFkappaB activation by LPS and T/I. Verbascoside and quercetin invariably impaired EGFR phosphorylation and UV-assocd. aryl hydrocarbon receptor (AhR)-mediated signaling, while rutin, polydatin and resveratrol did not affect EGFR phosphorylation and further activated AhR machinery in UV-exposed keratinocytes. In general, PPs down-regulated gene expression of pro-inflammatory cytokines/enzymes, except significant up-regulation of IL-8 obsd. under stimulation with TGFalpha. Both spontaneous and T/I-induced release of IL-8 and IP-10 was suppressed, although 50 μM resveratrol and polydatin up-regulated IL-8. At this concn., resveratrol activated both gene expression and de novo synthesis of IL-8 and AhR-mediated mechanisms were involved. We conclude that PPs differentially modulate the inflammatory response of human keratinocytes through distinct signal transduction pathways, including AhR and EGFR.
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18. 18
  Sinclair, D. A.; Guarente, L. Small-Molecule Allosteric Activators of Sirtuins. In Annual Review of Pharmacology and Toxicology, Vol 54; Insel, P. A., Ed.; Annual Reviews: Palo Alto, CA, 2014; Vol. 54, pp 363– 380.
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  Surh, Y. J. Cancer chemoprevention with dietary phytochemicals Nat. Rev. Cancer 2003, 3, 768– 780 DOI: 10.1038/nrc1189
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  Cancer chemoprevention with dietary phytochemicals
  Surh, Young-Joon
  Nature Reviews Cancer (2003), 3 (10), 768-780CODEN: NRCAC4; ISSN:1474-175X. (Nature Publishing Group)
  A review. Chemoprevention refers to the use of agents to inhibit, reverse or retard tumorigenesis. Numerous phytochems. derived from edible plants have been reported to interfere with a specific stage of the carcinogenic process. Many mechanisms have been shown to account for the anticarcinogenic actions of dietary constituents, but attention has recently been focused on intracellular-signaling cascades as common mol. targets for various chemopreventive phytochems.
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20. 20
  Ramos, S. Cancer chemoprevention and chemotherapy: Dietary polyphenols and signalling pathways Mol. Nutr. Food Res. 2008, 52, 507– 526 DOI: 10.1002/mnfr.200700326
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  Cancer chemoprevention and chemotherapy: dietary polyphenols and signalling pathways
  Ramos, Sonia
  Molecular Nutrition & Food Research (2008), 52 (5), 507-526CODEN: MNFRCV; ISSN:1613-4125. (Wiley-VCH Verlag GmbH & Co. KGaA)
  A review. Prevention of cancer through dietary intervention recently has received an increasing interest, and dietary polyphenols have become not only important potential chemopreventive, but also therapeutic, natural agents. Polyphenols have been reported to interfere at the initiation, promotion and progression of cancer. They might lead to the modulation of proteins in diverse pathways and require the integration of different signals for the final chemopreventive or therapeutic effect. Polyphenols have been demonstrated to act on multiple key elements in signal transduction pathways related to cellular proliferation, differentiation, apoptosis, inflammation, angiogenesis and metastasis; however, these mol. mechanisms of action are not completely characterized and many features remain to be elucidated. The aim of this review is to provide insights into the mol. basis of potential chemopreventive and therapeutic activities of dietary polyphenols with emphasis in their ability to control intracellular signaling cascades considered as relevant targets in a cancer preventive approach.
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  Seeram, N. P.; Zhang, Y. J.; Nair, M. G. Inhibition of proliferation of human cancer cells and cyclooxygenase enzymes by anthocyanidins and catechins Nutr. Cancer 2003, 46, 101– 106 DOI: 10.1207/S15327914NC4601_13
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  Inhibition of proliferation of human cancer cells and cyclooxygenase enzymes by anthocyanidins and catechins
  Seeram, Navindra P.; Zhang, Yanjun; Nair, Muraleedharan G.
  Nutrition and Cancer (2003), 46 (1), 101-106CODEN: NUCADQ; ISSN:0163-5581. (Lawrence Erlbaum Associates, Inc.)
  The widespread consumption of diets rich in anthocyanin and catechin content prompted the evaluation of their in vitro inhibitory effects on cyclooxygenase (COX) enzymes and on the proliferation of human cancer cell lines. Five anthocyanidins consisting of cyanidin (1), delphinidin (2), pelargonidin (3), peonidin (4), and malvidin (5) were tested for COX-1 and -2 enzyme inhibitory activities at 40 μM. Eleven catechins consisting of (+)-catechin (6), (-)-catechin (7), (±)-catechin (8), (+)-epicatechin (9), (-)-epicatechin (10), (-)-epigallocatechin (11), (-)-gallocatechin (12), (-)-epicatechin gallate (13), (-)-catechin gallate (14), (-)-epigallocatechin gallate (15), and (-)-gallocatechin gallate (16) were tested for inhibitory effects of COX-1 and -2 enzymes at 80 μM. Of the compds. tested, the galloyl derivs. of the catechins 11-15, cyanidin and malvidin , showed the best COX inhibitory activities compared with the com. anti-inflammatory drugs ibuprofen (at 10 μM), naproxen (at 10 μM), Vioxx (at 1.67 ppm), and Celebrex (at 1.67 ppm). Inhibition of the proliferation of the human cancer cell lines MCF-7 (breast), SF-268 (central nervous system, CNS), HCT-116 (colon), and NCI-H460 (lung) was evaluated at concns. between 100 and 6.25 μM compared with the com. std., adriamycin (doxorubicin) at 6.25 μM. At 100-μM concns., anthocyanidins 1-5 and catechins 6-10 did not inhibit proliferation of the four cell lines. At 50-μM concns., catechins 12, 15, and 16 showed 95%, 100%, and 97% inhibition of breast cells, resp. At 50-μM concns. 12 and 16 were the most effective catechins against colon cells (85% and 93%, resp.) and lung cells (87% and 67%, resp.). CNS cells were the most sensitive of the test cell lines, and total growth inhibition was obtained with catechins 12 and 16 at 100-μM concns. Overall, only the galloyl derivs. of catechins 11-16 inhibited the proliferation of the cancer cell lines.
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22. 22
  Xagorari, A.; Roussos, C.; Papapetropoulos, A. Inhibition of LPS-stimulated pathways in macrophages by the flavonoid luteolin Br. J. Pharmacol. 2002, 136, 1058– 1064 DOI: 10.1038/sj.bjp.0704803
  [ Crossref], [ PubMed], [ CAS], Google Scholar
  22
  Inhibition of LPS-stimulated pathways in macrophages by the flavonoid luteolin
  Xagorari, Angeliki; Roussos, Charis; Papapetropoulos, Andreas
  British Journal of Pharmacology (2002), 136 (7), 1058-1064CODEN: BJPCBM; ISSN:0007-1188. (Nature Publishing Group)
  1 We have previously shown that the flavonoid luteolin inhibits the expression of pro-inflammatory mols. induced by LPS. In the present study we tested the ability of luteolin to block signaling pathways implicated in LPS-induced inflammatory gene expression in macrophages. 2 Exposure of the murine macrophage cell line RAW 264.7 to LPS increased phosphorylation of the mitogen-activated protein kinase family members ERK1/2, p38 and JNK1/2 in a time-dependent manner. Pretreatment of RAW 264.7 with luteolin inhibited the LPS-induced ERK1/2 and p38, but not JNK1/2, phosphorylation, and blocked the LPS-induced TNF-α release. 3 To investigate which of these pathways contribute to the inhibitory effects of luteolin on TNF-α release, cells were pretreated with pharmacol. inhibitors of these pathways; PD98059 and SB203580 when used alone failed to inhibit TNF-α release, whereas pretreatment with both agents attenuated TNF-α release. 4 We have previously shown that luteolin blocks Akt phosphorylation in response to LPS in RAW 264.7 macrophages. To det. the role of Akt in TNF-α release, cells were transiently transfected with a dominant neg. form of Akt (K179M). Overexpression of K179M Akt did not alter LPS-induced TNF-α release, suggesting that inhibition of this kinase does not mediate the inhibitory action of luteolin. 5 In addn., DRB (a pharmacol. inhibitor of CK2) blocked TNF-α release in a concn.-dependent manner, whereas co-treatment of cells with luteolin and DRB did not have an additive effect. 6 We conclude that luteolin interferes with LPS signaling by reducing the activation of several MAPK family members and that its inhibitory action of TNF-α release correlates with inhibition of ERK, p38 and CK2 activation.
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23. 23
  Im, H.; Bantz, K. C.; Lee, S. H.; Johnson, T. W.; Haynes, C. L.; Oh, S.-H. Self-Assembled Plasmonic Nanoring Cavity Arrays for SERS and LSPR Biosensing Adv. Mater. 2013, 25, 2678– 2685 DOI: 10.1002/adma.201204283
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  23
  Self-Assembled Plasmonic Nanoring Cavity Arrays for SERS and LSPR Biosensing
  Im, Hyungsoon; Bantz, Kyle C.; Lee, Si Hoon; Johnson, Timothy W.; Haynes, Christy L.; Oh, Sang-Hyun
  Advanced Materials (Weinheim, Germany) (2013), 25 (19), 2678-2685CODEN: ADVMEW; ISSN:0935-9648. (Wiley-VCH Verlag GmbH & Co. KGaA)
  We have demonstrated a hybrid SERS substrate that combines the tunable LSPR of AgFON substrates with a strong field enhancement inside 10-nm metallic nanogaps. The increased LSPR sensitivity for surface-assocd. species makes the FON-gap substrate an ideal bioanal. platform to combine SERS and LSPR biosensing.
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24. 24
  Truong, P. L.; Kim, B. W.; Sim, S. J. Rational aspect ratio and suitable antibody coverage of gold nanorod for ultra-sensitive detection of a cancer biomarker Lab Chip 2012, 12, 1102– 1109 DOI: 10.1039/c2lc20588b
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  24
  Rational aspect ratio and suitable antibody coverage of gold nanorod for ultra-sensitive detection of a cancer biomarker
  Truong, Phuoc Long; Kim, Byung Woo; Sim, Sang Jun
  Lab on a Chip (2012), 12 (6), 1102-1109CODEN: LCAHAM; ISSN:1473-0189. (Royal Society of Chemistry)
  We report a simple, ultra-sensitive, and straightforward method for non-labeling detection of a cancer biomarker, using Rayleigh light scattering spectroscopy of the individual nanosensor based on antibody-antigen recognition and localized surface plasmon resonance (LSPR) λmax shifts. By exptl. measuring the refractive index sensitivity of Au nanorods, the Au nanorod with an aspect ratio of ∼3.5 was proven optimal for the LSPR sensing. To reduce the steric hindrance effect as well as to immobilize a large amt. of ligand on the nanoparticle surface, various mixts. contg. different molar ratios of HS(CH2)11(OCH2CH2)6OCH2COOH and HS(CH2)11(OCH2CH2)3OH were applied to form different self-assembled monolayer surfaces. The results showed that the best molar ratio for antibody conjugation was 1 : 10. When using individual Au nanorod sensors for the detection of prostate specific antigen (PSA), the lowest concn. recorded was ∼1 aM (∼6 × 105 mols.), corresponding to LSPR λmax shifts of ∼4.2 nm. These results indicate that sensor miniaturization down to the nanoscale level, the redn. of steric hindrance, and optimization of size, shape, and aspect ratio of nanorods have led to a significant improvement in the detection limit of sensors.
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25. 25
  Alivisatos, A. P.; Johnsson, K. P.; Peng, X. G.; Wilson, T. E.; Loweth, C. J.; Bruchez, M. P.; Schultz, P. G. Organization of ’nanocrystal molecules’ using DNA Nature 1996, 382, 609– 611 DOI: 10.1038/382609a0
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  25
  Organization of 'nanocrystal molecules' using DNA
  Alivisatos, A. Paul; Johnsson, Kai P.; Peng, Xiaogang; Wilson, Troy E.; Loweth, Colin J.; Bruchez, Marcel P., Jr.; Schultz, Peter G.
  Nature (London) (1996), 382 (6592), 609-611CODEN: NATUAS; ISSN:0028-0836. (Macmillan Magazines)
  The authors describe a strategy for the synthesis of 'nanocrystal mols.', in which discrete nos. of Au nanocrystals are organized into spatially defined structures based on Watson-Crick base-pairing interactions. The authors attach single-stranded DNA oligonucleotides of defined length and sequence to individual nanocrystals, and these assemble into dimers and trimers on addn. of a complementary single-stranded DNA template. The authors anticipate that this approach should allow the construction of more complex two- and three-dimensional assemblies.
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26. 26
  Wu, B.; Chen, L. C.; Huang, Y. J.; Zhang, Y. M.; Kang, Y. J.; Kim, D. H. Multiplexed Biomolecular Detection Based on Single Nanoparticles Immobilized on Pneumatically Controlled Microfluidic Chip Plasmonics 2014, 9, 801– 807 DOI: 10.1007/s11468-013-9661-4
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  26
  Multiplexed Biomolecular Detection Based on Single Nanoparticles Immobilized on Pneumatically Controlled Microfluidic Chip
  Wu, Bo; Chen, Li-Chan; Huang, Youju; Zhang, Yiming; Kang, Yuejun; Kim, Dong-Hwan
  Plasmonics (2014), 9 (4), 801-807CODEN: PLASCS; ISSN:1557-1955. (Springer)
  A microfluidic chip integrated with pneumatically controlled valves was developed for multiplexed biomol. detection via localized surface plasmonic resonance (LSPR) of single gold nanorod. The cost-effective microfluidic chip was assembled by polydimethylsiloxane layers and glass substrates with a precisely controlled thickness. The thin and flat microfluidic chip fitted the narrow space of dark-field microscopy and enabled the recording of single-nanoparticle LSPR responses. Aptamer-antigen-antibody sandwiched detection scheme was utilized to enhance the LSPR responses for label-free biomol. detection. This microfluidic chip successfully demonstrated the multiplexed detection of three independent analytes (PSA, IgE, and thrombin).
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27. 27
  Balamurugan, S.; Mayer, K. M.; Lee, S.; Soper, S. A.; Hafner, J. H.; Spivak, D. A. Nanostructure shape effects on response of plasmonic aptamer sensors J. Mol. Recognit. 2013, 26, 402– 407 DOI: 10.1002/jmr.2278
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  Nanostructure shape effects on response of plasmonic aptamer sensors
  Balamurugan, Subramanian; Mayer, Kathryn M.; Lee, Seunghyun; Soper, Steven A.; Hafner, Jason H.; Spivak, David A.
  Journal of Molecular Recognition (2013), 26 (9), 402-407CODEN: JMORE4; ISSN:0952-3499. (Wiley-Blackwell)
  A localized surface plasmon resonance (LSPR) sensor surface was fabricated by the deposition of gold nanorods on a glass substrate and subsequent immobilization of the DNA aptamer, which specifically bind to thrombin. This LSPR aptamer sensor showed a response of 6-nm λmax shift for protein binding with the detection limit of at least 10pM, indicating one of the highest sensitivities achieved for thrombin detection by optical extinction LSPR. We also tested the LSPR sensor fabricated using gold bipyramid, which showed higher refractive index sensitivity than the gold nanorods, but the overall response of gold bipyramid sensor appears to be 25% less than that of the gold nanorod substrate, despite the approx. twofold higher refractive index sensitivity. XPS anal. showed that this is due to the low surface d. of aptamers on the gold bipyramid compared with gold nanorods. The low surface d. of the aptamers on the gold bipyramid surface may be due to the effect of shape of the nanostructure on the kinetics of aptamer monolayer formation. The small size of aptamers relative to other bioreceptors is the key to achieving high sensitivity by biosensors on the basis of LSPR, demonstrated here for protein binding. The generality of aptamer sensors for protein detection using gold nanorod and gold nanobipyramid substrates is anticipated to have a large impact in the important development of sensors toward biomarkers, environmental toxins, and warfare agents. Copyright © 2013 John Wiley & Sons, Ltd.
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28. 28
  Bhagawati, M.; You, C. J.; Piehler, J. Quantitative Real-Time Imaging of Protein-Protein Interactions by LSPR Detection with Micropatterned Gold Nanoparticles Anal. Chem. 2013, 85, 9564– 9571 DOI: 10.1021/ac401673e
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  28
  Quantitative Real-Time Imaging of Protein-Protein Interactions by LSPR Detection with Micropatterned Gold Nanoparticles
  Bhagawati, Maniraj; You, Changjiang; Piehler, Jacob
  Analytical Chemistry (Washington, DC, United States) (2013), 85 (20), 9564-9571CODEN: ANCHAM; ISSN:0003-2700. (American Chemical Society)
  Localized surface plasmon resonance (LSPR) offers powerful means for sensitive label-free detection of protein-protein interactions in a highly multiplexed format. The authors have here established self-assembly and surface modification of plasmonic nanostructures on solid support suitable for quant. protein-protein interaction anal. by spectroscopic and microscopic LSPR detection. These architectures were obtained by layer-by-layer assembly via electrostatic attraction. Gold nanoparticles (AuNP) were adsorbed on a biocompatible amine-terminated poly-(ethylene glycol) (PEG) polymer brush and further functionalized by poly-L-lysine graft PEG (PLL-PEG) copolymers. Stable yet reversible protein immobilization was achieved via tris-(nitrilotriacetic acid) groups incorporated into the PLL-PEG coating. Thus, site-specific immobilization of His-tagged proteins via complexed Ni(II) ions was achieved. Functional protein immobilization on the surface was confirmed by real-time detection of LSPR scattering by reflectance spectroscopy. Assocn. and dissocn. rate consts. obtained for a reversible protein-protein interaction were in good agreement with the data obtained by other surface-sensitive detection techniques. For spatially resolved detection, AuNP were assembled into micropatterns by photolithog. uncaging of surface amines. LSPR imaging of reversible protein-protein interactions was possible in a conventional wide field microscope, yielding detection limits of ∼30 protein mols. within a diffraction-limited surface area.
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29. 29
  Cohavi, O.; Reichmann, D.; Abramovich, R.; Tesler, A. B.; Bellapadrona, G.; Kokh, D. B.; Wade, R. C.; Vaskevich, A.; Rubinstein, I.; Schreiber, G. A Quantitative, Real-Time Assessment of Binding of Peptides and Proteins to Gold Surfaces Chem. - Eur. J. 2011, 17, 1327– 1336 DOI: 10.1002/chem.201001781
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  A Quantitative, Real-Time Assessment of Binding of Peptides and Proteins to Gold Surfaces
  Cohavi, Ori; Reichmann, Dana; Abramovich, Renne; Tesler, Alexander B.; Bellapadrona, Giuliano; Kokh, Daria B.; Wade, Rebecca C.; Vaskevich, Alexander; Rubinstein, Israel; Schreiber, Gideon
  Chemistry - A European Journal (2011), 17 (4), 1327-1336, S1327/1-S1327/7CODEN: CEUJED; ISSN:0947-6539. (Wiley-VCH Verlag GmbH & Co. KGaA)
  Interactions of peptides and proteins with inorg. surfaces are important to both natural and artificial systems; however, a detailed understanding of such interactions is lacking. In this study, we applied new approaches to quant. measure the binding of amino acids and proteins to gold surfaces. Real-time surface plasmon resonance (SPR) measurements showed that TEM1-β-lactamase inhibitor protein (BLIP) interacts only weakly with Au nanoparticles (NPs). However, fusion of three histidine residues to BLIP (3H-BLIP) resulted in a significant increase in the binding to the Au NPs, which further increased when the histidine tail was extended to six histidines (6H-BLIP). Further increasing the no. of His residues had no effect on the binding. A parallel study using continuous (111)-textured Au surfaces and single-cryst., (111)-oriented, Au islands by ellipsometry, FTIR, and localized surface plasmon resonance (LSPR) spectroscopy further confirmed the results, validating the broad applicability of Au NPs as model surfaces. Evaluating the binding of all other natural amino acid homotripeptides fused to BLIP (except Cys and Pro) showed that arom. and pos.-charged residues bind preferentially to Au with respect to small aliph. and neg. charged residues, and that the rate of assocn. is related to the potency of binding. The binding of all fusions was irreversible. These findings were substantiated by SPR measurements of synthesized, free, sol. tripeptides using Au-NP-modified SPR chips. Here, however, the binding was reversible allowing for detn. of binding affinities that correlate with the binding potencies of the related BLIP fusions. Competition assays performed between 3H-BLIP and the histidine tripeptide (3 His) suggest that Au binding residues promote the adsorption of proteins on the surface, and by this facilitate the irreversible interaction of the polypeptide chain with Au. The binding of amino acids to Au was simulated by using a continuum solvent model, showing agreement with the exptl. values. These results, together with the obsd. binding potencies and kinetics of the BLIP fusions and free peptides, suggest a binding mechanism that is markedly different from biol. protein-protein interactions.
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30. 30
  Chen, S.; Svedendahl, M.; Van Duyne, R. P.; Kall, M. Plasmon-Enhanced Colorimetric ELISA with Single Molecule Sensitivity Nano Lett. 2011, 11, 1826– 1830 DOI: 10.1021/nl2006092
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  30
  Plasmon-Enhanced Colorimetric ELISA with Single Molecule Sensitivity
  Chen, Si; Svedendahl, Mikael; Van Duyne, Richard P.; Kaell, Mikael
  Nano Letters (2011), 11 (4), 1826-1830CODEN: NALEFD; ISSN:1530-6984. (American Chemical Society)
  Robust but ultrasensitive biosensors with a capability of detecting low abundance biomarkers could revolutionize clin. diagnostics and enable early detection of cancer, neurol. diseases, and infections. The authors utilized a combination of localized surface plasmon resonance (LSPR) refractive index sensing and the well-known ELISA to develop a simple colorimetric biosensing methodol. with single mol. sensitivity. The technique is based on spectral imaging of a large no. of isolated gold nanoparticles. Each particle binds a variable no. of horseradish peroxidase (HRP) enzyme mols. that catalyze a localized pptn. reaction at the particle surface. The enzymic reaction dramatically amplifies the shift of the LSPR scattering max., λmax, and makes it possible to detect the presence of only one or a few HRP mols. per particle.
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31. 31
  Zhang, J.; Wang, L.; Pan, D.; Song, S.; Boey, F. Y. C.; Zhang, H.; Fan, C. Visual cocaine detection with gold nanoparticles and rationally engineered aptamer structures Small 2008, 4, 1196– 1200 DOI: 10.1002/smll.200800057
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  31
  Visual cocaine detection with gold nanoparticles and rationally engineered aptamer structures
  Zhang, Juan; Wang, Lihua; Pan, Dun; Song, Shiping; Boey, Freddy Y. C.; Zhang, Hua; Fan, Chunhai
  Small (2008), 4 (8), 1196-1200CODEN: SMALBC; ISSN:1613-6810. (Wiley-VCH Verlag GmbH & Co. KGaA)
  A bioassay strategy is designed to detect small-mol. targets such as cocaine, potassium, and adenosine, based on gold nanoparticles and engineered DNA aptamers. In this design, an aptamer is engineered to be two pieces of random, coil-like single-stranded DNA, which reassembles into the intact aptamer tertiary structure in the presence of the specific target. Au nanoparticles can effectively differentiate between these two states via their characteristic surface-plasmon resonance-based color change. Using this method, cocaine in the low-micromolar range is selectively detected within minutes. This strategy is also generic and applicable to the detection of several other small-mol. targets.
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32. 32
  Guerreiro, J. R. L.; Frederiksen, M.; Bochenkov, V. E.; De Freitas, V.; Ferreira Sales, M. G.; Sutherland, D. S. Multifunctional Biosensor Based on Localized Surface Plasmon Resonance for Monitoring Small Molecule-Protein Interaction ACS Nano 2014, 8, 7958– 7967 DOI: 10.1021/nn501962y
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  32
  Multifunctional Biosensor Based on Localized Surface Plasmon Resonance for Monitoring Small Molecule-Protein Interaction
  Guerreiro, Joana Rafaela Lara; Frederiksen, Maj; Bochenkov, Vladimir E.; De Freitas, Victor; Ferreira Sales, Maria Goreti; Sutherland, Duncan Steward
  ACS Nano (2014), 8 (8), 7958-7967CODEN: ANCAC3; ISSN:1936-0851. (American Chemical Society)
  We report an optical sensor based on localized surface plasmon resonance (LSPR) to study small-mol. protein interaction combining high sensitivity refractive index sensing for quant. binding information and subsequent conformation-sensitive plasmon-activated CD spectroscopy. The interaction of α-amylase and a small-size mol. (PGG, pentagalloyl glucose) was log concn.-dependent from 0.5 to 154 μM. In situ tests were addnl. successfully applied to the anal. of real wine samples. These studies demonstrate that LSPR sensors to monitor small mol.-protein interactions in real time and in situ, which is a great advance within technol. platforms for drug discovery.
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33. 33
  Chianella, I.; Guerreiro, A.; Moczko, E.; Caygill, J. S.; Piletska, E. V.; De Vargas Sansalvador, I. M.; Whitcombe, M. J.; Piletsky, S. A. Direct Replacement of Antibodies with Molecularly Imprinted Polymer Nanoparticles in ELISA-Development of a Novel Assay for Vancomycin Anal. Chem. 2013, 85, 8462– 8468 DOI: 10.1021/ac402102j
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  33
  Direct Replacement of Antibodies with Molecularly Imprinted Polymer Nanoparticles in ELISA-Development of a Novel Assay for Vancomycin
  Chianella, Iva; Guerreiro, Antonio; Moczko, Ewa; Caygill, J. Sarah; Piletska, Elena V.; De Vargas Sansalvador, Isabel M. Perez; Whitcombe, Michael J.; Piletsky, Sergey A.
  Analytical Chemistry (Washington, DC, United States) (2013), 85 (17), 8462-8468CODEN: ANCHAM; ISSN:0003-2700. (American Chemical Society)
  A simple and straightforward technique for coating microplate wells with molecularly imprinted polymer nanoparticles (nanoMIPs) to develop assays similar to the ELISA is presented here for the first time. NanoMIPs were synthesized by a solid-phase approach with an immobilized vancomycin (template) and characterized using Biacore 3000, dynamic light scattering, and electron microscopy. Immobilization, blocking, and washing conditions were optimized in microplate format. The detection of vancomycin was achieved in competitive binding expts. with a horseradish peroxidase-vancomycin conjugate. The assay was capable of measuring vancomycin in buffer and in blood plasma within the range of 0.001-70 nM with a detection limit of 0.0025 nM (2.5 pM). The sensitivity of the assay was 3 orders of magnitude better than a previously described ELISA based on antibodies. In these expts., nanoMIPs showed high affinity and minimal interference from blood plasma components. Immobilized nanoMIPs were stored for 1 mo at room temp. without any detrimental effects to their binding properties. The high affinity of nanoMIPs and the lack of a requirement for cold chain logistics make them an attractive alternative to traditional antibodies used in ELISA.
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34. 34
  Abbas, A.; Tian, L. M.; Morrissey, J. J.; Kharasch, E. D.; Singamaneni, S. Hot Spot-Localized Artificial Antibodies for Label-Free Plasmonic Biosensing Adv. Funct. Mater. 2013, 23, 1789– 1797 DOI: 10.1002/adfm.201202370
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  34
  Hot Spot-Localized Artificial Antibodies for Label-Free Plasmonic Biosensing
  Abbas, Abdennour; Tian, Limei; Morrissey, Jeremiah J.; Kharasch, Evan D.; Singamaneni, Srikanth
  Advanced Functional Materials (2013), 23 (14), 1789-1797CODEN: AFMDC6; ISSN:1616-301X. (Wiley-VCH Verlag GmbH & Co. KGaA)
  The development of biomol. imprinting over the last decade has raised promising perspectives in replacing natural antibodies with artificial antibodies. A significant no. of reports have been dedicated to imprinting of org. and inorg. nanostructures, but very few were performed on nanomaterials with a transduction function. Herein, a relatively fast and efficient plasmonic hot spot-localized surface imprinting of gold nanorods using reversible template immobilization and siloxane copolymn. is described. The technique enables a fine control of the imprinting process at the nanometer scale and provides a nanobiosensor with high selectivity and reusability. Proof of concept was established by the detection of neutrophil gelatinase-assocd. lipocalin (NGAL), a biomarker for acute kidney injury, using localized surface plasmon resonance spectroscopy. The work represents a valuable step towards plasmonic nanobiosensors with synthetic antibodies for label-free and cost-efficient diagnostic assays. It is expected that this novel class of surface imprinted plasmonic nanomaterials will open up new possibilities in advancing biomedical applications of plasmonic nanostructures.
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35. 35
  Fredriksson, H.; Alaverdyan, Y.; Dmitriev, A.; Langhammer, C.; Sutherland, D. S.; Zaech, M.; Kasemo, B. Hole-mask colloidal lithography Adv. Mater. 2007, 19, 4297– 4302 DOI: 10.1002/adma.200700680
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  Hole-mask colloidal lithography
  Fredriksson, Hans; Alaverdyan, Yury; Dmitriev, Alexandre; Langhammer, Christoph; Sutherland, Duncan S.; Zaech, Michael; Kasemo, Bengt
  Advanced Materials (Weinheim, Germany) (2007), 19 (23), 4297-4302CODEN: ADVMEW; ISSN:0935-9648. (Wiley-VCH Verlag GmbH & Co. KGaA)
  Hole-mask colloidal lithog. represents a truly versatile and simple bottom-up nanofabrication method based on colloidal self-assembly lithog. patterning. The technique provides an effective means of patterning vast surface areas with diverse functional nanoarchitectures. Examples include arrays of nanodisks, oriented elliptical nanostructures, (binary) nanodisk pairs, nanocones on extended surfaces and nanodisks embedded in a surrounding matrix.
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  Whitcombe, M. J.; Chianella, I.; Larcombe, L.; Piletsky, S. A.; Noble, J.; Porter, R.; Horgan, A. The rational development of molecularly imprinted polymer-based sensors for protein detection Chem. Soc. Rev. 2011, 40, 1547– 1571 DOI: 10.1039/C0CS00049C
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  A review. The detection of specific proteins as biomarkers of disease, health status, environmental monitoring, food quality, control of fermenters and civil defense purposes means that biosensors for these targets will become increasingly more important. Among the technologies used for building specific recognition properties, molecularly imprinted polymers (MIPs) are attracting much attention. In this crit. review we describe many methods used for imprinting recognition for protein targets in polymers and their incorporation with a no. of transducer platforms with the aim of identifying the most promising approaches for the prepn. of MIP-based protein sensors (277 refs.).
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  Biosensors & Bioelectronics (2013), 45 (), 237-244CODEN: BBIOE4; ISSN:0956-5663. (Elsevier B.V.)
  This work introduces two major changes to the conventional protocol for designing plastic antibodies: (i) the imprinted sites were created with charged monomers while the surrounding environment was tailored using neutral material; and (ii) the protein was removed from its imprinted site by means of a protease, aiming at preserving the polymeric network of the plastic antibody. To our knowledge, these approaches were never presented before and the resulting material was named here as smart plastic antibody material (SPAM). As proof of concept, SPAM was tailored on top of disposable gold-screen printed electrodes (Au-SPE), following a bottom-up approach, for targeting myoglobin (Myo) in a point-of-care context. The existence of imprinted sites was checked by comparing a SPAM modified surface to a neg. control, consisting of similar material where the template was omitted from the procedure and called non-imprinted materials (NIMs). All stages of the creation of the SPAM and NIM on the Au layer were followed by both electrochem. impedance spectroscopy (EIS) and cyclic voltammetry (CV). AFM imaging was also performed to characterize the topog. of the surface. There are two major reasons supporting the fact that plastic antibodies were effectively designed by the above approach: (i) they were visualized for the first time by AFM, being present only in the SPAM network; and (ii) only the SPAM material was able to rebind to the target protein and produce a linear elec. response against EIS and square wave voltammetry (SWV) assays, with NIMs showing a similar-to-random behavior. The SPAM/Au-SPE devices displayed linear responses to Myo in EIS and SWV assays down to 3.5 μg/mL and 0.58 μg/mL, resp., with detection limits of 1.5 and 0.28 μg/mL. SPAM materials also showed negligible interference from troponin T (TnT), bovine serum albumin (BSA) and urea under SWV assays, showing promising results for point-of-care applications when applied to spiked biol. fluids.
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  Mazzotta, F.; Johnson, T. W.; Dahlin, A. B.; Shaver, J.; Oh, S.-H.; Höök, F. Influence of the evanescent field decay length on the sensitivity of plasmonic nanodisks and nanoholes ACS Photonics 2015, 2, 256– 262 DOI: 10.1021/ph500360d
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  ACS Photonics (2015), 2 (2), 256-262CODEN: APCHD5; ISSN:2330-4022. (American Chemical Society)
  We evaluate and compare the sensitivity of gold nanodisks on silica substrates and nanoholes made in silica-supported gold films, two of the most common sensor structures used in plasmonic biosensing. An alumina overcoat was applied by at. layer deposition (ALD) to precisely control the interfacial refractive index and det. the evanescent plasmonic field decay length. The results are in good agreement with anal. models and biomol. binding expts. for the two substrates. We found that nanodisks outperform nanoholes for thin dielec. coatings (<∼20 nm), while the opposite holds true for thicker coatings (>∼20 nm). The optimum nanoplasmonic transducer element for a given biorecognition reaction can be chosen based on exptl. detd. bulk sensitivities/noise levels and theor. estd. evanescent field decay lengths.
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  Cardenas, Marite; Arnebrant, Thomas; Rennie, Adrian; Fragneto, Giovanna; Thomas, Robert K.; Lindh, Liselott
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  Films formed from saliva on surfaces are important for the maintenance of oral health and integrity by protection against chem. and/or biol. agents. The aim of the present study was to investigate adsorbed amts., thickness, and structure of films formed from human whole saliva on alumina surfaces by means of in situ ellipsometry, neutron reflectivity, and at. force microscopy. Alumina (Al2O3, synthetic sapphire) is a relevant and interesting substrate for saliva adsorption studies as it has an isoelec. point close to that of tooth enamel. The results showed that saliva adsorbs rapidly on alumina. The film could be modeled in two layers: an inner and dense thin region that forms a uniform layer and an outer, more diffuse and thicker region that protrudes toward the bulk of the soln. The film morphol. described a uniformly covering dense layer and a second outer layer contg. polydisperse adsorbed macromols. or aggregates.
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  Hook, F.; Voros, J.; Rodahl, M.; Kurrat, R.; Boni, P.; Ramsden, J. J.; Textor, M.; Spencer, N. D.; Tengvall, P.; Gold, J.; Kasemo, B. A comparative study of protein adsorption on titanium oxide surfaces using in situ ellipsometry, optical waveguide lightmode spectroscopy, and quartz crystal microbalance/dissipation Colloids Surf., B 2002, 24, 155– 170 DOI: 10.1016/S0927-7765(01)00236-3
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  A comparative study of protein adsorption on titanium oxide surfaces using in situ ellipsometry, optical waveguide lightmode spectroscopy, and quartz crystal microbalance/dissipation
  Hook, F.; Voros, J.; Rodahl, M.; Kurrat, R.; Boni, P.; Ramsden, J. J.; Textor, M.; Spencer, N. D.; Tengvall, P.; Gold, J.; Kasemo, B.
  Colloids and Surfaces, B: Biointerfaces (2002), 24 (2), 155-170CODEN: CSBBEQ; ISSN:0927-7765. (Elsevier Science B.V.)
  The adsorption kinetics of three model proteins--human serum albumin, fibrinogen and Hb--has been measured and compared using three different exptl. techniques: optical waveguide lightmode spectroscopy (OWLS), ellipsometry (ELM) and quartz crystal microbalance (QCM-D). The studies were complemented by also monitoring the corresponding antibody interactions with the pre-adsorbed protein layer. All measurements were performed with identically prepd. titanium oxide coated substrates. All three techniques are suitable to follow in-situ kinetics of protein-surface and protein-antibody interactions, and provide quant. values of the adsorbed adlayer mass. The results have, however, different phys. contents. The optical techniques OWLS and ELM provide in most cases consistent and comparable results, which can be straightforwardly converted to adsorbed protein molar ('dry') mass. QCM-D, produces measured values that are generally higher in terms of mass. This, in turn, provides valuable, complementary information in two respects: (i) the mass calcd. from the resonance frequency shift includes both protein mass and water that binds or hydrodynamically couples to the protein adlayer; and (ii) anal. of the energy dissipation in the adlayer and its magnitude in relation to the frequency shift (c.f. adsorbed mass) provides insight about the mech./structural properties such as viscoelasticity.
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The Supporting Information is available free of charge on the ACS Publications website at DOI: 10.1021/acssensors.5b00054.
- Materials and methods including saliva characterization, Au nanodisks fabrication, molecular imprinted synthesis, and evaluation, interaction measurements by LSPR, electrochemical measurements, as well as description of data analysis; bare Au disks MIP and nonimprinted layer characterized by atomic force microscopy; mass spectroscopy of both pure saliva and Au disks/MIP saliva/rebinding saliva (PDF)
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Molecular Imprinting of Complex Matrices at Localized Surface Plasmon Resonance Biosensors for Screening of Global Interactions of Polyphenols and Proteins

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Abstract

Experimental Section

Au Nanodisks Fabrication

Molecular Imprinted Films

LSPR Interaction Studies in a Flow System

Results and Discussion

Molecular Imprinting Procedure on Au Nanodisks

Figure 1

Figure 2

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Rebinding Capability

FDTD Calculations

Figure 4

Binding Affinities

Figure 5

Conclusions

Supporting Information

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Terms & Conditions

Acknowledgment

References

Cited By

Abstract

Figure 1

Figure 2

Figure 3

Figure 4

Figure 5

References

Supporting Information

Supporting Information

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