Conformational changes of peptides at solid/liquid interfaces: a Monte Carlo study.
Monte Carlo simulations were performed to study the conformational changes of negatively charged model peptides dissolved in water adsorbed onto charged surfaces. 8-, 16-, and 20-residues peptides were used, each of them consisted of repeating diblock units of aspartic acid (ASP, polar amino acid) and isoleucine (ILE, nonpolar amino acid) residues. We found that a water patch was retained at the charged surface, separating the peptide from it. We believed that these water molecules were primarily responsible for giving a particular orientation to the peptide at the surface. Water did play a role to some extent in the structural stability of the 8-residues peptide. However, for higher chain lengths (16-residues and 20-residues), the intrinsic hydrogen-bonding network (or intrinsic structural stability) showed a predominant effect over hydrophobic dehydration for the stability of the peptide at the surface.
Mungikar
Amol A
AA
Chemical and Biological Engineering Department, University of Missouri-Rolla, Rolla, Missouri 65409, USA.
Forciniti
Daniel
D
D000327:Adsorption; D055592:Biophysical Phenomena; D001703:Biophysics; D006860:Hydrogen Bonding; D046911:Macromolecular Substances / Q000737:chemistry*; D008958:Models, Molecular; D015233:Models, Statistical; D008962:Models, Theoretical; D008968:Molecular Conformation; D009010:Monte Carlo Method; D010100:Oxygen / Q000737:chemistry; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D055672:Static Electricity; D014867:Water / Q000737:chemistry
D046911:Macromolecular Substances; D010455:Peptides; D014867:Water; D010100:Oxygen