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Orientation of Biotin-Binding Sites in Streptavidin Adsorbed onto the Surface of Polythiophene Films

  • Kamil Awsiuk*
    Kamil Awsiuk
    M. Smoluchowski Institute of Physics, Jagiellonian University, Łojasiewicza 11, 30-348 Kraków, Poland
    Institute of Nuclear & Radiological Sciences & Technology, Energy & Safety, NCSR Demokritos, 15310 Agia Paraskevi, Greece
    *E-mail: [email protected]. Tel: +48 12 664 4557. Fax: +48 12 664 4905.
    More by Kamil Awsiuk
  • Panagiota Petrou
    Panagiota Petrou
    Institute of Nuclear & Radiological Sciences & Technology, Energy & Safety, NCSR Demokritos, 15310 Agia Paraskevi, Greece
  • Angelos Thanassoulas
    Angelos Thanassoulas
    Institute of Nuclear & Radiological Sciences & Technology, Energy & Safety, NCSR Demokritos, 15310 Agia Paraskevi, Greece
  • , and 
  • Joanna Raczkowska
    Joanna Raczkowska
    M. Smoluchowski Institute of Physics, Jagiellonian University, Łojasiewicza 11, 30-348 Kraków, Poland
Cite this: Langmuir 2019, 35, 8, 3058–3066
Publication Date (Web):January 30, 2019
https://doi.org/10.1021/acs.langmuir.8b03509
Copyright © 2019 American Chemical Society

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    Abstract

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    The orientation of biotin-binding sites of streptavidin adsorbed to thin films of three polythiophenes (PTs), namely, regioregular poly(3-hexylthiophene) (RP3HT), regiorandom poly(3-butylthiophene) (P3BT), and poly(3,3‴-didodecylquaterthiophene) (PQT12), has been investigated. Polymer films were examined prior to and after protein adsorption with atomic force microscopy and time-of-flight secondary ion mass spectrometry (ToF-SIMS). Principal component analysis (PCA) applied to ToF-SIMS data revealed subtle changes in surface chemistry of polymer films and orientation of adsorbed streptavidin. PCA resolved the surface alignment of alkyl side chains and differentiated the ToF-SIMS data for PQT12, RP3HT, and P3BT, verifying an amorphous morphology for P3BT and a semicrystalline one for PQT12 and RP3HT. After the characterization of the polymeric films, streptavidin adsorption from solutions with different protein concentrations (up to 300 μg/mL) has been conducted. The PCA results distinguished between amino acids characteristic for external regions of streptavidin molecules adsorbed to different PTs suggest that streptavidin adsorbed to PQT12 exposes molecular regions rich in tryptophan and tyrosine, which are components of the biotin-binding sites. The latter results were confirmed using biotin-labeled horse radish peroxidase to estimate the exposed binding sites of streptavidin adsorbed onto the different PT films. The analysis of streptavidin structure suggests that interaction between polythiophene film and dipole moment of streptavidin subunit is responsible for orientation of biotin-binding sites.

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    The Supporting Information is available free of charge on the ACS Publications website at DOI: 10.1021/acs.langmuir.8b03509.

    • Negative-ion ToF-SIMS spectra of P3BT, RP3HT, and PQT12 surfaces; table of ToF-SIMS signals selected for PCA from mass spectra of polythiophene thin films prior to protein adsorption; normalized intensities of ToF-SIMS signal originating from tryptophan collected from streptavidin adsorbed onto the surface of different polythiophenes; table of ToF-SIMS signals selected for PCA from mass spectra of streptavidin adsorbed to polythiophene thin films, their mass, and amino acid origin; hydrophobicity of amino acid side chains against loadings on PC2 (PDF)

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    Cited By

    This article is cited by 8 publications.

    1. Boonya Thongrom, Mathias Dimde, Uwe Schedler, Rainer Haag. Thiol‐Click Based Polyglycerol Hydrogels as Biosensing Platform with In Situ Encapsulated Streptavidin Probes. Macromolecular Chemistry and Physics 2023, 224 (1) , 2200271. https://doi.org/10.1002/macp.202200271
    2. Katarzyna Gajos, Andrzej Budkowski, Panagiota Petrou, Sotirios Kakabakos. A perspective on ToF-SIMS analysis of biosensor interfaces: Controlling and optimizing multi-molecular composition, immobilization through bioprinting, molecular orientation. Applied Surface Science 2022, 594 , 153439. https://doi.org/10.1016/j.apsusc.2022.153439
    3. Kamil Awsiuk, Paweł Dąbczyński, Mateusz M. Marzec, Jakub Rysz, Ellen Moons, Andrzej Budkowski. Electrically Switchable Film Structure of Conjugated Polymer Composites. Materials 2022, 15 (6) , 2219. https://doi.org/10.3390/ma15062219
    4. Autumn Carlsen, Vincent Tabard‐Cossa. Mapping shifts in nanopore signal to changes in protein and protein‐DNA conformation. PROTEOMICS 2022, 22 (5-6) https://doi.org/10.1002/pmic.202100068
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    6. Katarzyna Gajos, Kamil Awsiuk, Andrzej Budkowski. Controlling orientation, conformation, and biorecognition of proteins on silane monolayers, conjugate polymers, and thermo-responsive polymer brushes: investigations using TOF-SIMS and principal component analysis. Colloid and Polymer Science 2021, 299 (3) , 385-405. https://doi.org/10.1007/s00396-020-04711-7
    7. Jane Zveiter Moraes, Bárbara Hamaguchi, Camila Braggion, Enzo Reina Speciale, Fernanda Beatriz Viana Cesar, Gabriela de Fátima da Silva Soares, Juliana Harumi Osaki, Tauane Mathias Pereira, Rodrigo Barbosa Aguiar. Hybridoma technology: is it still useful?. Current Research in Immunology 2021, 2 , 32-40. https://doi.org/10.1016/j.crimmu.2021.03.002
    8. Agnieszka Kamińska, Katarzyna Gajos, Olga Woźnicka, Anna Dłubacz, Magdalena E. Marzec, Andrzej Budkowski, Ewa Ł. Stępień. Using a lactadherin-immobilized silicon surface for capturing and monitoring plasma microvesicles as a foundation for diagnostic device development. Analytical and Bioanalytical Chemistry 2020, 412 (29) , 8093-8106. https://doi.org/10.1007/s00216-020-02938-5

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