Conformational Changes of Peptides at Solid/Liquid Interfaces: A Monte Carlo Study
Abstract
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.
Recommended Citation
A. A. Mungikar and D. Forciniti, "Conformational Changes of Peptides at Solid/Liquid Interfaces: A Monte Carlo Study," Biomacromolecules, American Chemical Society (ACS), Sep 2004.
The definitive version is available at https://doi.org/10.1021/bm049808s
Department(s)
Chemical and Biochemical Engineering
Sponsor(s)
National Science Foundation (U.S.)
Keywords and Phrases
Aspartic Acid; Diblock Units; Hydrophobic Dehydration; Peptides
International Standard Serial Number (ISSN)
1525-7797
Document Type
Article - Journal
Document Version
Citation
File Type
text
Language(s)
English
Rights
© 2004 American Chemical Society (ACS), All rights reserved.
Publication Date
25 Sep 2004
