Polypeptide friction and adhesion on hydrophobic and hydrophilic surfaces: a molecular dynamics case study.
Using all-atomistic MD simulations including explicit water, the mobility and adhesion of a mildly hydrophobic single polypeptide chain adsorbed on hydrophobic and hydrophilic diamond surfaces is investigated by application of lateral and vertical pulling forces. Forced motion on the hydrophilic surface exhibits stick-slip due to breaking and reformation of hydrogen bonds; in contrast, on the hydrophobic surface, the motion is smooth. By carefully tuning the driving force magnitude, the linear-response regime is reached on a hydrophobic surface and equilibrium values for mobility and adhesive strength are obtained. On the hydrophilic surface, on the other hand, slow hydrogen-bond kinetics prevents equilibration and only upper bounds for adhesion force and mobility can be estimated. Whereas the desorption force is rather comparable on the two surfaces and differs at most by a factor of 2, the mobility on the hydrophilic surface is at least 30-fold reduced compared to the hydrophobic one. A simple model based on a single particle diffusing in a corrugated potential landscape suggests that cooperativity is rather limited and that the small mobility on a hydrophilic surface can be rationalized in terms of incoherently moving monomers. The experimentally well-known peptide mobility in bulk water is quantitatively reproduced in our simulations, which serves as a sensitive test on our methodology employed.
Serr
Andreas
A
Physik Department, Technische Universität München, 85748 Garching, Germany.
Horinek
Dominik
D
Netz
Roland R
RR
D000327:Adsorption; D000595:Amino Acid Sequence; D003198:Computer Simulation; D017276:Friction; D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D013499:Surface Properties
D010455:Peptides