ACS Publications. Most Trusted. Most Cited. Most Read
CONTENT TYPES

Figure 1Loading Img

System Message

The ACS Publications site will be temporarily unavailable for planned maintenance on Friday, Oct. 15 starting at 6:00 pm ET for up to 4 hours. We apologize for this inconvenience.

Self-Assembly of Ovalbumin into Amyloid and Non-Amyloid Fibrils

View Author Information
Food and Soft Material Science, Institute of Food, Nutrition and Health, ETH Zürich, Schmelzbergstrasse 9, LFO E 23, 8092 Zürich, Switzerland
Cite this: Biomacromolecules 2012, 13, 12, 4213–4221
Publication Date (Web):October 25, 2012
https://doi.org/10.1021/bm301481v
Copyright © 2012 American Chemical Society
Article Views
2446
Altmetric
-
Citations
LEARN ABOUT THESE METRICS
Read OnlinePDF (2 MB)
Supporting Info (1)»

Abstract

Abstract Image

We study the fibrillation pathway of ovalbumin protein and report the simultaneous formation of several types of fibrils, with clear structural and physical differences. We compare the fibrillation mechanisms at low pH with and without salt, and follow the kinetics of fibrils growth by atomic force microscopy (AFM), static and dynamic light scattering (SLS, DLS), and small-angle X-ray scattering (SAXS). We show that, among the morphologies identified, long semiflexible amyloid fibrils (type I), with persistence length Lp ∼ 3 μm, Young's modulus E ∼ 2.8 GPa, and cross-β structure are formed. We also observe much more flexible fibrils (type III, Lp ∼ 63 nm), that can assemble into multistranded ribbons with time. They show significantly lower intrinsic stiffness (1.1 GPa) and a secondary structure, which is not characteristic of the well-ordered amyloids, as determined by circular dichroism (CD), wide-angle X-ray scattering (WAXS), and attenuated total reflectance Fourier transform infrared spectroscopy (ATR-FTIR). In between these two main classes of fibrils, a third family, with intermediate flexibility (type II, Lp ∼ 300 nm), is also resolved.

Supporting Information

ARTICLE SECTIONS
Jump To

Supplementary figures: AFM height images, SDS-PAGE, MALDI-MS, and FTIR results. Comparison of the theoretical and experimental Rg and Rh. SAXS fitting model. This material is available free of charge via the Internet at http://pubs.acs.org.

Terms & Conditions

Most electronic Supporting Information files are available without a subscription to ACS Web Editions. Such files may be downloaded by article for research use (if there is a public use license linked to the relevant article, that license may permit other uses). Permission may be obtained from ACS for other uses through requests via the RightsLink permission system: http://pubs.acs.org/page/copyright/permissions.html.

Cited By


This article is cited by 80 publications.

  1. Mohammad Peydayesh, Toni Suta, Mattia Usuelli, Stephan Handschin, Greta Canelli, Massimo Bagnani, Raffaele Mezzenga. Sustainable Removal of Microplastics and Natural Organic Matter from Water by Coagulation–Flocculation with Protein Amyloid Fibrils. Environmental Science & Technology 2021, 55 (13) , 8848-8858. https://doi.org/10.1021/acs.est.1c01918
  2. Rocío Jurado, Jozef Adamcik, Antoni Sánchez-Ferrer, Sreenath Bolisetty, Raffaele Mezzenga, Natividad Gálvez. Understanding the Formation of Apoferritin Amyloid Fibrils. Biomacromolecules 2021, 22 (5) , 2057-2066. https://doi.org/10.1021/acs.biomac.1c00176
  3. Da Chen, Naagarajan Narayanan, Enrico Federici, Zhi Yang, Xiaobing Zuo, Jinling Gao, Fang Fang, Meng Deng, Osvaldo H. Campanella, Owen G. Jones. Electrospinning Induced Orientation of Protein Fibrils. Biomacromolecules 2020, 21 (7) , 2772-2785. https://doi.org/10.1021/acs.biomac.0c00500
  4. Margarita Monge-Morera, Marlies A. Lambrecht, Lomme J. Deleu, Rodrigo Gallardo, Nikolaos N. Louros, Matthias De Vleeschouwer, Frederic Rousseau, Joost Schymkowitz, Jan A. Delcour. Processing Induced Changes in Food Proteins: Amyloid Formation during Boiling of Hen Egg White. Biomacromolecules 2020, 21 (6) , 2218-2228. https://doi.org/10.1021/acs.biomac.0c00186
  5. Wei Ji, Chengqian Yuan, Shai Zilberzwige-Tal, Ruirui Xing, Priyadarshi Chakraborty, Kai Tao, Sharon Gilead, Xuehai Yan, Ehud Gazit. Metal-Ion Modulated Structural Transformation of Amyloid-Like Dipeptide Supramolecular Self-Assembly. ACS Nano 2019, 13 (6) , 7300-7309. https://doi.org/10.1021/acsnano.9b03444
  6. Masahiro Noji, Masatomo So, Keiichi Yamaguchi, Hironobu Hojo, Maki Onda, Yoko Akazawa-Ogawa, Yoshihisa Hagihara, Yuji Goto. Heat-Induced Aggregation of Hen Ovalbumin Suggests a Key Factor Responsible for Serpin Polymerization. Biochemistry 2018, 57 (37) , 5415-5426. https://doi.org/10.1021/acs.biochem.8b00619
  7. Christian Helbing, Tanja Deckert-Gaudig, Izabela Firkowska-Boden, Gang Wei, Volker Deckert, and Klaus D. Jandt . Protein Handshake on the Nanoscale: How Albumin and Hemoglobin Self-Assemble into Nanohybrid Fibers. ACS Nano 2018, 12 (2) , 1211-1219. https://doi.org/10.1021/acsnano.7b07196
  8. Koen J. A. Jansens, Kristof Brijs, Jörg Stetefeld, Jan A. Delcour, and Martin G. Scanlon . Ultrasonic Characterization of Amyloid-Like Ovalbumin Aggregation. ACS Omega 2017, 2 (8) , 4612-4620. https://doi.org/10.1021/acsomega.7b00366
  9. Alberto Gonzalez-Jordan, Taco Nicolai, and Lazhar Benyahia . Influence of the Protein Particle Morphology and Partitioning on the Behavior of Particle-Stabilized Water-in-Water Emulsions. Langmuir 2016, 32 (28) , 7189-7197. https://doi.org/10.1021/acs.langmuir.6b01993
  10. Jianguo Zhao, Sreenath Bolisetty, Jozef Adamcik, Jun Han, María P. Fernández-Ronco, and Raffaele Mezzenga . Freeze–Thaw Cycling Induced Isotropic–Nematic Coexistence of Amyloid Fibrils Suspensions. Langmuir 2016, 32 (10) , 2492-2499. https://doi.org/10.1021/acs.langmuir.6b00276
  11. Gurbir Singh and Tejwant Singh Kang . Ionic Liquid Surfactant Mediated Structural Transitions and Self-Assembly of Bovine Serum Albumin in Aqueous Media: Effect of Functionalization of Ionic Liquid Surfactants. The Journal of Physical Chemistry B 2015, 119 (33) , 10573-10585. https://doi.org/10.1021/acs.jpcb.5b04854
  12. Mily Bhattacharya and Priyanka Dogra . Self-Assembly of Ovalbumin Amyloid Pores: Effects on Membrane Permeabilization, Dipole Potential, and Bilayer Fluidity. Langmuir 2015, 31 (32) , 8911-8922. https://doi.org/10.1021/acs.langmuir.5b02074
  13. Jay Gilbert, Osvaldo Campanella, and Owen G. Jones . Electrostatic Stabilization of β-lactoglobulin Fibrils at Increased pH with Cationic Polymers. Biomacromolecules 2014, 15 (8) , 3119-3127. https://doi.org/10.1021/bm500762u
  14. Ivan Usov, Jozef Adamcik, and Raffaele Mezzenga . Polymorphism Complexity and Handedness Inversion in Serum Albumin Amyloid Fibrils. ACS Nano 2013, 7 (12) , 10465-10474. https://doi.org/10.1021/nn404886k
  15. Yuki Kawachi, Rina Kameyama, Akihiro Handa, Nobuyuki Takahashi, and Naoki Tanaka . Role of the N-Terminal Amphiphilic Region of Ovalbumin during Heat-Induced Aggregation and Gelation. Journal of Agricultural and Food Chemistry 2013, 61 (36) , 8668-8675. https://doi.org/10.1021/jf402456v
  16. Gang Liu and Qixin Zhong . Dispersible and Thermal Stable Nanofibrils Derived from Glycated Whey Protein. Biomacromolecules 2013, 14 (7) , 2146-2153. https://doi.org/10.1021/bm400521b
  17. Anna Hu, Liang Li. Effect mechanism of ultrasound pretreatment on fibrillation Kinetics, physicochemical properties and structure characteristics of soy protein isolate nanofibrils. Ultrasonics Sonochemistry 2021, 78 , 105741. https://doi.org/10.1016/j.ultsonch.2021.105741
  18. Sauradipta Banerjee. Modification with N-benzylisatin restricts stress-induced aggregation of hen egg white lysozyme: Anti-amyloidogenic property of isatin derivative with possible clinical implications. International Journal of Biological Macromolecules 2021, 187 , 341-349. https://doi.org/10.1016/j.ijbiomac.2021.07.092
  19. Stephani Stamboroski, Arundhati Joshi, Paul‐Ludwig Michael Noeske, Susan Köppen, Dorothea Brüggemann. Principles of Fibrinogen Fiber Assembly In Vitro. Macromolecular Bioscience 2021, 21 (5) , 2000412. https://doi.org/10.1002/mabi.202000412
  20. G. Rathod, J.K. Amamcharla. Process development for a novel milk protein concentrate with whey proteins as fibrils. Journal of Dairy Science 2021, 104 (4) , 4094-4107. https://doi.org/10.3168/jds.2020-19409
  21. Nicole Balasco, Carlo Diaferia, Giancarlo Morelli, Luigi Vitagliano, Antonella Accardo. Amyloid-Like Aggregation in Diseases and Biomaterials: Osmosis of Structural Information. Frontiers in Bioengineering and Biotechnology 2021, 9 https://doi.org/10.3389/fbioe.2021.641372
  22. Sauradipta Banerjee. Long-term incubation of myoglobin with glyoxal induces amyloid like aggregation of the heme protein: Implications of advanced glycation end products in protein conformational disorders. Journal of Molecular Liquids 2021, 326 , 115256. https://doi.org/10.1016/j.molliq.2020.115256
  23. Arne M.R. Huyst, Lomme J. Deleu, Trui Luyckx, Marlies A. Lambrecht, John Van Camp, Jan A. Delcour, Paul Van der Meeren. Influence of hydrophobic interfaces and shear on ovalbumin amyloid-like fibril formation in oil-in-water emulsions. Food Hydrocolloids 2021, 111 , 106327. https://doi.org/10.1016/j.foodhyd.2020.106327
  24. Govindarajan Prasanna, Pu Jing. Polyphenol binding disassembles glycation-modified bovine serum albumin amyloid fibrils. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 2021, 246 , 119001. https://doi.org/10.1016/j.saa.2020.119001
  25. Sauradipta Banerjee. Methylglyoxal modification reduces the sensitivity of hen egg white lysozyme to stress-induced aggregation: Insight into the anti-amyloidogenic property of α-dicarbonyl compound. Journal of Biomolecular Structure and Dynamics 2020, 38 (18) , 5474-5487. https://doi.org/10.1080/07391102.2019.1702589
  26. Sauradipta Banerjee. RETRACTED ARTICLE: Glyoxal modification mediates conformational alterations in silk fibroin: Induction of fibrillation with amyloidal features. Journal of Biosciences 2020, 45 (1) https://doi.org/10.1007/s12038-020-0009-x
  27. Govindarajan Prasanna, Pu Jing. Polyphenols redirects the self-assembly of serum albumin into hybrid nanostructures. International Journal of Biological Macromolecules 2020, 164 , 3932-3942. https://doi.org/10.1016/j.ijbiomac.2020.09.005
  28. Nicoletta Giamblanco, Jean‐Marc Janot, Alberto Gubbiotti, Mauro Chinappi, Sebastien Balme. Characterization of Food Amyloid Protein Digestion by Conical Nanopore. Small Methods 2020, 4 (11) , 1900703. https://doi.org/10.1002/smtd.201900703
  29. Takashi Hiroi, Kazu Hirosawa, Yuya Okazumi, Sai Venkatesh Pingali, Mitsuhiro Shibayama. Mechanism of heat-induced gelation for ovalbumin under acidic conditions and the effect of peptides. Polymer Journal 2020, 52 (11) , 1263-1272. https://doi.org/10.1038/s41428-020-0382-1
  30. Di An, Liang Li. The Effect of Limited Proteolysis by Trypsin on the Formation of Soy Protein Isolate Nanofibrils. Journal of Chemistry 2020, 2020 , 1-12. https://doi.org/10.1155/2020/8185037
  31. Farhad Alavi, Zahra Emam-Djomeh, Mehdi Mohammadian, Maryam Salami, Ali Akbar Moosavi-Movahedi. Physico-chemical and foaming properties of nanofibrillated egg white protein and its functionality in meringue batter. Food Hydrocolloids 2020, 101 , 105554. https://doi.org/10.1016/j.foodhyd.2019.105554
  32. Chunjun Yan, Zheng Zhou. Ellagic acid can act as a chaperone and suppress the heat-induced amyloid-like aggregation of ovalbumin. Food Hydrocolloids 2020, 100 , 105408. https://doi.org/10.1016/j.foodhyd.2019.105408
  33. Jelica Milošević, Jovan Petrić, Branko Jovčić, Brankica Janković, Natalija Polović. Exploring the potential of infrared spectroscopy in qualitative and quantitative monitoring of ovalbumin amyloid fibrillation. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 2020, 229 , 117882. https://doi.org/10.1016/j.saa.2019.117882
  34. Christian Helbing, Klaus D. Jandt. Novel protein and peptide nanofibrous structures via supramolecular co-assembly. 2020,,, 69-97. https://doi.org/10.1016/B978-0-08-102850-6.00004-8
  35. Yu Hu, Chengxin He, Meng Wai Woo, Hua Xiong, Juwu Hu, Qiang Zhao. Formation of fibrils derived from whey protein isolate: structural characteristics and protease resistance. Food & Function 2019, 10 (12) , 8106-8115. https://doi.org/10.1039/C9FO00961B
  36. Jubong Lee, Ji-Hye Lee, Seung R. Paik, Bongjun Yeom, Kookheon Char. Thermally triggered self-assembly of κ-casein amyloid nanofibrils and their nanomechanical properties. Polymer 2019, 179 , 121626. https://doi.org/10.1016/j.polymer.2019.121626
  37. Yiping Cao, Raffaele Mezzenga. Food protein amyloid fibrils: Origin, structure, formation, characterization, applications and health implications. Advances in Colloid and Interface Science 2019, 269 , 334-356. https://doi.org/10.1016/j.cis.2019.05.002
  38. Koen J.A. Jansens, Marlies A. Lambrecht, Ine Rombouts, Margarita Monge Morera, Kristof Brijs, Frederic Rousseau, Joost Schymkowitz, Jan A. Delcour. Conditions Governing Food Protein Amyloid Fibril Formation—Part I: Egg and Cereal Proteins. Comprehensive Reviews in Food Science and Food Safety 2019, 18 (4) , 1256-1276. https://doi.org/10.1111/1541-4337.12462
  39. Leila Josefsson, Melker Cronhamn, Malin Ekman, Hugo Widehammar, Åsa Emmer, Christofer Lendel. Structural basis for the formation of soy protein nanofibrils. RSC Advances 2019, 9 (11) , 6310-6319. https://doi.org/10.1039/C8RA10610J
  40. Sara La Manna, Valentina Roviello, Pasqualina Liana Scognamiglio, Carlo Diaferia, Cinzia Giannini, Teresa Sibillano, Giancarlo Morelli, Ettore Novellino, Daniela Marasco. Amyloid fibers deriving from the aromatic core of C-terminal domain of nucleophosmin 1. International Journal of Biological Macromolecules 2019, 122 , 517-525. https://doi.org/10.1016/j.ijbiomac.2018.10.210
  41. Özgenur Coşkun, İbrahim Gülseren. Nanofibrils of beta-lactoglobulin for encapsulation of food ingredients. 2019,,, 125-146. https://doi.org/10.1016/B978-0-12-815663-6.00005-7
  42. Xinchen Ye, Christofer Lendel, Maud Langton, Richard T. Olsson, Mikael S. Hedenqvist. Protein nanofibrils: Preparation, properties, and possible applications in industrial nanomaterials. 2019,,, 29-63. https://doi.org/10.1016/B978-0-12-815749-7.00002-5
  43. Koen J.A. Jansens, Ine Rombouts, Charlotte Grootaert, Kristof Brijs, John Van Camp, Paul Van der Meeren, Frederic Rousseau, Joost Schymkowitz, Jan A. Delcour. Rational Design of Amyloid-Like Fibrillary Structures for Tailoring Food Protein Techno-Functionality and Their Potential Health Implications. Comprehensive Reviews in Food Science and Food Safety 2019, 18 (1) , 84-105. https://doi.org/10.1111/1541-4337.12404
  44. Aleksandr Kakinen, Jozef Adamcik, Bo Wang, Xinwei Ge, Raffaele Mezzenga, Thomas P. Davis, Feng Ding, Pu Chun Ke. Nanoscale inhibition of polymorphic and ambidextrous IAPP amyloid aggregation with small molecules. Nano Research 2018, 11 (7) , 3636-3647. https://doi.org/10.1007/s12274-017-1930-7
  45. Saba Tufail, Mohd. Asif Sherwani, Shoaib Shoaib, Sarfuddin Azmi, Mohammad Owais, Najmul Islam. Ovalbumin self-assembles into amyloid nanosheets that elicit immune responses and facilitate sustained drug release. Journal of Biological Chemistry 2018, 293 (29) , 11310-11324. https://doi.org/10.1074/jbc.RA118.002550
  46. E. Vahdat-Ahar, A. A. Moosavi-Movahedi, F. Taghavi, M. Habibi-Rezaei, N. Sheibani. Lag phase alteration in the modified bovine serum albumin under the inducing and inhibitory effect of vitamin C. Journal of the Iranian Chemical Society 2018, 15 (6) , 1337-1346. https://doi.org/10.1007/s13738-018-1332-0
  47. Anna Kharlamova, Taco Nicolai, Christophe Chassenieux. Calcium-induced gelation of whey protein aggregates: Kinetics, structure and rheological properties. Food Hydrocolloids 2018, 79 , 145-157. https://doi.org/10.1016/j.foodhyd.2017.11.049
  48. Wensi Zhang, Xiaoqing Yu, Yang Li, Zhiqiang Su, Klaus D. Jandt, Gang Wei. Protein-mimetic peptide nanofibers: Motif design, self-assembly synthesis, and sequence-specific biomedical applications. Progress in Polymer Science 2018, 80 , 94-124. https://doi.org/10.1016/j.progpolymsci.2017.12.001
  49. Ulyana Shimanovich, Dorothea Pinotsi, Klimentiy Shimanovich, Na Yu, Sreenath Bolisetty, Jozef Adamcik, Raffaele Mezzenga, Jerome Charmet, Fritz Vollrath, Ehud Gazit, Christopher M. Dobson, Gabriele Kaminski Schierle, Chris Holland, Clemens F. Kaminski, Tuomas P. J. Knowles. Biophotonics of Native Silk Fibrils. Macromolecular Bioscience 2018, 18 (4) , 1700295. https://doi.org/10.1002/mabi.201700295
  50. Raphaela Araujo Mantovani, Guilherme de Figueiredo Furtado, Flavia Maria Netto, Rosiane Lopes Cunha. Assessing the potential of whey protein fibril as emulsifier. Journal of Food Engineering 2018, 223 , 99-108. https://doi.org/10.1016/j.jfoodeng.2017.12.006
  51. Xinchen Ye, Mikael S. Hedenqvist, Maud Langton, Christofer Lendel. On the role of peptide hydrolysis for fibrillation kinetics and amyloid fibril morphology. RSC Advances 2018, 8 (13) , 6915-6924. https://doi.org/10.1039/C7RA10981D
  52. Paola Cicatiello, Principia Dardano, Marinella Pirozzi, Alfredo M. Gravagnuolo, Luca De Stefano, Paola Giardina. Self-assembly of two hydrophobins from marine fungi affected by interaction with surfaces. Biotechnology and Bioengineering 2017, 114 (10) , 2173-2186. https://doi.org/10.1002/bit.26344
  53. Fatemeh Rashno, Khosro Khajeh, Claudia Capitini, Reza H. Sajedi, Maryam Monsef Shokri, Fabrizio Chiti. Very rapid amyloid fibril formation by a bacterial lipase in the absence of a detectable lag phase. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 2017, 1865 (6) , 652-663. https://doi.org/10.1016/j.bbapap.2017.03.004
  54. Anna Russo, Carlo Diaferia, Sara La Manna, Cinzia Giannini, Teresa Sibillano, Antonella Accardo, Giancarlo Morelli, Ettore Novellino, Daniela Marasco. Insights into amyloid-like aggregation of H2 region of the C-terminal domain of nucleophosmin. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 2017, 1865 (2) , 176-185. https://doi.org/10.1016/j.bbapap.2016.11.006
  55. Gang Wei, Zhiqiang Su, Nicholas P. Reynolds, Paolo Arosio, Ian W. Hamley, Ehud Gazit, Raffaele Mezzenga. Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology. Chemical Society Reviews 2017, 46 (15) , 4661-4708. https://doi.org/10.1039/C6CS00542J
  56. Koen J.A. Jansens, Kristof Brijs, Jan A. Delcour, Martin G. Scanlon. Amyloid-like aggregation of ovalbumin: Effect of disulfide reduction and other egg white proteins. Food Hydrocolloids 2016, 61 , 914-922. https://doi.org/10.1016/j.foodhyd.2016.07.015
  57. Sauradipta Banerjee, Abhay Sankar Chakraborti. Glyoxal administration induces formation of high molecular weight aggregates of hemoglobin exhibiting amyloidal nature in experimental rats: An in vivo study. International Journal of Biological Macromolecules 2016, 93 , 805-813. https://doi.org/10.1016/j.ijbiomac.2016.09.061
  58. Abolfazl Jangholi, Mohammad Reza Ashrafi-Kooshk, Seyed Shahriar Arab, Gholamhossein Riazi, Farzad Mokhtari, Mansour Poorebrahim, Hamid Mahdiuni, Boris I. Kurganov, Ali Akbar Moosavi-Movahedi, Reza Khodarahmi. Appraisal of role of the polyanionic inducer length on amyloid formation by 412-residue 1N4R Tau protein: A comparative study. Archives of Biochemistry and Biophysics 2016, 609 , 1-19. https://doi.org/10.1016/j.abb.2016.09.004
  59. M. Mučibabić, M.M. Apetri, G.W. Canters, T.J. Aartsma. The effect of fluorescent labeling on α-synuclein fibril morphology. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 2016, 1864 (10) , 1419-1427. https://doi.org/10.1016/j.bbapap.2016.07.007
  60. Ruchuan Liu, Qinqiu Deng, Zhen Yang, Daiwen Yang, Ming-Yong Han, Xiang Yang Liu. “Nano-Fishnet” Structure Making Silk Fibers Tougher. Advanced Functional Materials 2016, 26 (30) , 5534-5541. https://doi.org/10.1002/adfm.201600813
  61. Wenfei Xiong, Yuntao Wang, Chunlan Zhang, Jiawei Wan, Bakht Ramin Shah, Yaqiong Pei, Bin Zhou, Jin Li, Bin Li. High intensity ultrasound modified ovalbumin: Structure, interface and gelation properties. Ultrasonics Sonochemistry 2016, 31 , 302-309. https://doi.org/10.1016/j.ultsonch.2016.01.014
  62. Maria Gaczynska, Przemyslaw Karpowicz, Christine E. Stuart, Malgorzata G. Norton, Jeffrey H. Teckman, Ewa Marszal, Pawel A. Osmulski, . AFM Imaging Reveals Topographic Diversity of Wild Type and Z Variant Polymers of Human α1-Proteinase Inhibitor. PLOS ONE 2016, 11 (3) , e0151902. https://doi.org/10.1371/journal.pone.0151902
  63. Kang Pan, Qixin Zhong. Organic Nanoparticles in Foods: Fabrication, Characterization, and Utilization. Annual Review of Food Science and Technology 2016, 7 (1) , 245-266. https://doi.org/10.1146/annurev-food-041715-033215
  64. Sauradipta Banerjee, Subhajit Maity, Abhay Sankar Chakraborti. Methylglyoxal-induced modification causes aggregation of myoglobin. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 2016, 155 , 1-10. https://doi.org/10.1016/j.saa.2015.10.022
  65. O. N. Koroleva, E. V. Dubrovin, A. P. Tolstova, N. V. Kuzmina, T. V. Laptinskaya, I. V. Yaminsky, V. L. Drutsa. A hypothetical hierarchical mechanism of the self-assembly of the Escherichia coli RNA polymerase σ 70 subunit. Soft Matter 2016, 12 (7) , 1974-1982. https://doi.org/10.1039/C5SM02934A
  66. Irina Portnaya, Sharon Avni, Ellina Kesselman, Yoav Boyarski, Shahar Sukenik, Daniel Harries, Nily Dan, Uri Cogan, Dganit Danino. Competing processes of micellization and fibrillization in native and reduced casein proteins. Physical Chemistry Chemical Physics 2016, 18 (32) , 22516-22525. https://doi.org/10.1039/C6CP04582K
  67. Lisa R. Volpatti, Ulyana Shimanovich, Francesco Simone Ruggeri, Sreenath Bolisetty, Thomas Müller, Thomas O. Mason, Thomas C. T. Michaels, Raffaele Mezzenga, Giovanni Dietler, Tuomas P. J. Knowles. Micro- and nanoscale hierarchical structure of core–shell protein microgels. Journal of Materials Chemistry B 2016, 4 (48) , 7989-7999. https://doi.org/10.1039/C6TB02683D
  68. Jason M.D. Kalapothakis, Ryan J. Morris, Juraj Szavits-Nossan, Kym Eden, Sam Covill, Sean Tabor, Jay Gillam, Perdita E. Barran, Rosalind J. Allen, Cait E. MacPhee. A Kinetic Study of Ovalbumin Fibril Formation: The Importance of Fragmentation and End-Joining. Biophysical Journal 2015, 108 (9) , 2300-2311. https://doi.org/10.1016/j.bpj.2015.03.021
  69. Dong-Ju You, Ju Huck Lee, Jin Young Kim, Gil-Ja Jhon, Hyun Suk Jung. Effect of nitric oxide on conformational changes of ovalbumin accompanying self-assembly into non-disease-associated fibrils. Nitric Oxide 2015, 47 , 1-9. https://doi.org/10.1016/j.niox.2015.02.004
  70. Francesco Simone Ruggeri, Jozef Adamcik, Jae Sun Jeong, Hilal A. Lashuel, Raffaele Mezzenga, Giovanni Dietler. Influence of the β-Sheet Content on the Mechanical Properties of Aggregates during Amyloid Fibrillization. Angewandte Chemie 2015, 127 (8) , 2492-2496. https://doi.org/10.1002/ange.201409050
  71. Francesco Simone Ruggeri, Jozef Adamcik, Jae Sun Jeong, Hilal A. Lashuel, Raffaele Mezzenga, Giovanni Dietler. Influence of the β-Sheet Content on the Mechanical Properties of Aggregates during Amyloid Fibrillization. Angewandte Chemie International Edition 2015, 54 (8) , 2462-2466. https://doi.org/10.1002/anie.201409050
  72. Kang Pan, Qixin Zhong. Amyloid-like fibrils formed from intrinsically disordered caseins: physicochemical and nanomechanical properties. Soft Matter 2015, 11 (29) , 5898-5904. https://doi.org/10.1039/C5SM01037C
  73. Arshdeep Sidhu, Ine Segers-Nolten, Vinod Subramaniam. Solution conditions define morphological homogeneity of α-synuclein fibrils. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 2014, 1844 (12) , 2127-2134. https://doi.org/10.1016/j.bbapap.2014.09.007
  74. Pui Yeu Phoon, Maria Fernanda San Martin-Gonzalez, Ganesan Narsimhan. Effect of hydrolysis of soy β-conglycinin on the oxidative stability of O/W emulsions. Food Hydrocolloids 2014, 35 , 429-443. https://doi.org/10.1016/j.foodhyd.2013.06.024
  75. Lisa R. Volpatti, Tuomas P. J. Knowles. Polymer physics inspired approaches for the study of the mechanical properties of amyloid fibrils. Journal of Polymer Science Part B: Polymer Physics 2014, 52 (4) , 281-292. https://doi.org/10.1002/polb.23428
  76. Elke Scholten, Thomas Moschakis, Costas G. Biliaderis. Biopolymer composites for engineering food structures to control product functionality. Food Structure 2014, 1 (1) , 39-54. https://doi.org/10.1016/j.foostr.2013.11.001
  77. Yu-Zhe Gao, Hong-Hua Xu, Ting-Ting Ju, Xin-Huai Zhao. The effect of limited proteolysis by different proteases on the formation of whey protein fibrils. Journal of Dairy Science 2013, 96 (12) , 7383-7392. https://doi.org/10.3168/jds.2013-6843
  78. Taco Nicolai, Dominique Durand. Controlled food protein aggregation for new functionality. Current Opinion in Colloid & Interface Science 2013, 18 (4) , 249-256. https://doi.org/10.1016/j.cocis.2013.03.001
  79. Wiwat Nuansing, Daniela Frauchiger, Florian Huth, Amaia Rebollo, Rainer Hillenbrand, Alexander M. Bittner. Electrospinning of peptide and protein fibres: approaching the molecular scale. Faraday Discussions 2013, 166 , 209. https://doi.org/10.1039/c3fd00069a
  80. Ivan Usov, Jozef Adamcik, Raffaele Mezzenga. Polymorphism in bovine serum albumin fibrils: morphology and statistical analysis. Faraday Discussions 2013, 166 , 151. https://doi.org/10.1039/c3fd00083d

Pair your accounts.

Export articles to Mendeley

Get article recommendations from ACS based on references in your Mendeley library.

Pair your accounts.

Export articles to Mendeley

Get article recommendations from ACS based on references in your Mendeley library.

You’ve supercharged your research process with ACS and Mendeley!

STEP 1:
Click to create an ACS ID

Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

MENDELEY PAIRING EXPIRED
Your Mendeley pairing has expired. Please reconnect

This website uses cookies to improve your user experience. By continuing to use the site, you are accepting our use of cookies. Read the ACS privacy policy.

CONTINUE