Schwierz, Nadine and Horinek, Dominik and Liese, Susanne and Pirzer, Tobias and Balzer, Bizan N. and Hugel, Thorsten and Netz, Roland R. (2012) On the Relationship between Peptide Adsorption Resistance and Surface Contact Angle: A Combined Experimental and Simulation Single-Molecule Study. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 134 (48). pp. 19628-19638. ISSN 0002-7863,
Full text not available from this repository. (Request a copy)Abstract
The force-induced desorption of single peptide chains from mixed OH/CH3-terminated self-assembled monolayers is studied in closely matched molecular dynamics simulations and atomic force microscopy experiments with the goal to gain microscopic understanding of the transition between peptide adsorption and adsorption resistance as the surface contact angle is varied. In both simulations and 5 I experiments, the surfaces become adsorption resistant against hydrophilic as well as hydrophobic peptides when their contact angle decreases below theta approximate to 50 degrees-60 degrees, thus confirming the so-called Berg limit established in the context of protein and cell adsorption. Entropy/enthalpy decomposition of the simulation results reveals that the key discriminator between the adsorption of different residues on a hydrophobic monolayer is of entropic nature and thus is suggested to be linked to the hydrophobic effect. By pushing a polyalanine peptide onto a polar surface, simulations reveal that the peptide adsorption resistance is caused by the strongly bound water hydration layer and characterized by the simultaneous gain of both total entropy in the system and total number of hydrogen bonds between water, peptide, and surface. This mechanistic insight into peptide adsorption resistance might help to refine design principles for anti-fouling surfaces.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | SELF-ASSEMBLED MONOLAYERS; PROTEIN ADSORPTION; HYDROPHILIC SURFACES; INTERFACIAL WATER; ADHESION STRENGTH; FORCE MICROSCOPY; FREE-ENERGY; THERMODYNAMICS; HYDROPHOBICITY; WETTABILITY; |
| Subjects: | 500 Science > 540 Chemistry & allied sciences |
| Divisions: | Chemistry and Pharmacy > Institut für Physikalische und Theoretische Chemie Chemistry and Pharmacy > Institut für Physikalische und Theoretische Chemie > Chair of Chemistry VI - Physical Chemistry (Solution Chemistry) Chemistry and Pharmacy > Institut für Physikalische und Theoretische Chemie > Chair of Chemistry VI - Physical Chemistry (Solution Chemistry) > Prof. Dr. Dominik Horinek |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 30 Apr 2020 12:15 |
| Last Modified: | 30 Apr 2020 12:15 |
| URI: | https://pred.uni-regensburg.de/id/eprint/17609 |
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