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  Controlling Amphipathic Peptide Adsorption by Smart Switchable Germanium Interfaces

Baumgartner, L.-M., Erbe, A., Boyle, A. L., & Rabe, M. (2022). Controlling Amphipathic Peptide Adsorption by Smart Switchable Germanium Interfaces. Physical Chemistry Chemical Physics, -. doi:10.1039/D1CP03938E.

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Controlling Amphipathic Peptide Adsorption by Smart.pdf (Publisher version), 4MB
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2022
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 Creators:
Baumgartner, Laura-Marleen1, Author              
Erbe, Andreas1, 2, Author              
Boyle, Aimee L.3, Author              
Rabe, Martin1, Author              
Affiliations:
1Interface Spectroscopy, Interface Chemistry and Surface Engineering, Max-Planck-Institut für Eisenforschung GmbH, Max Planck Society, ou_1863358              
2Department of Materials Science and Engineering, NTNU - Norwegian University of Science and Technology, 7491 Trondheim, Norway, ou_persistent22              
3Leiden Institute of Chemistry, Leiden University, Einsteinweg 55, 2333 CC Leiden, The Netherlands, ou_persistent22              

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 Abstract: The in situ control of reversible protein adsorption to a surface is a critical step towards biofouling prevention and finds utilisation in bioanalytical applications. In this work,} adsorption of peptides is controlled by employing the electrode potential induced{,} reversible change of germanium (100) surface termination between a hydrophobic{,} hydrogen terminated and a hydrophilic{,} hydroxyl terminated surface. This simple but effective {'}smart{'} interface is used to direct adsorption of two peptides models{,} representing the naturally highly abundant structural motifs of amphipathic helices and coiled-coils. Their structural similarity coincides with their opposite overall charge and hence allows the examination of the influence of charge and hydrophobicity on adsorption. Polarized attenuated total reflection infrared (ATR-IR) spectroscopy at controlled electrode potential has been used to follow the adsorption process at physiological \pH\ in deuterated buffer. The delicate balance of hydrophobic and electrostatic peptide/surface interactions leads to two different processes upon switching that are both observed in situ: reversible adsorption and reversible reorientation. Negatively charged peptide adsorption can be fully controlled by switching to the hydrophobic interface{,} while the same switch causes the positively charged helical peptide to tilt down. This principle can be used for {'}smart{'} adsorption control of a wider variety of proteins and peptides and hence find application{, e.g. as a bioanalytical tool or functional biosensors.

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Language(s): eng - English
 Dates: 2022-02-022022
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Type: -
 Identifiers: DOI: 10.1039/D1CP03938E
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Title: Physical Chemistry Chemical Physics
  Abbreviation : Phys. Chem. Chem. Phys.
Source Genre: Journal
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Publ. Info: Cambridge, England : Royal Society of Chemistry
Pages: 12 Volume / Issue: - Sequence Number: - Start / End Page: - Identifier: ISSN: 1463-9076
CoNE: https://pure.mpg.de/cone/journals/resource/954925272413_1