Peptide adsorption on a hydrophobic surface results from an interplay of solvation, surface, and intrapeptide forces.

ABSTRACT: The hydrophobic effect, i.e., the poor solvation of nonpolar parts of molecules, plays a key role in protein folding and more generally for molecular self-assembly and aggregation in aqueous media. The perturbation of the water structure accounts for many aspects of protein hydrophobicity. However, to what extent the dispersion interaction between molecular entities themselves contributes has remained unclear. This is so because in peptide folding interactions and structural changes occur on all length scales and make disentangling various contributions impossible. We address this issue both experimentally and theoretically by looking at the force necessary to peel a mildly hydrophobic single peptide molecule from a flat hydrophobic diamond surface in the presence of water. This setup avoi

SUBMITTER: Horinek D 

PROVIDER: S-EPMC2268547 | biostudies-literature | 2008 Feb

REPOSITORIES: biostudies-literature