Interactions of cationic-hydrophobic peptides with lipid bilayers: a Monte Carlo simulation method.

ABSTRACT: We present a computational model of the interaction between hydrophobic cations, such as the antimicrobial peptide, Magainin2, and membranes that include anionic lipids. The peptide's amino acids were represented as two interaction sites: one corresponds to the backbone alpha-carbon and the other to the side chain. The membrane was represented as a hydrophobic profile, and its anionic nature was represented by a surface of smeared charges. Thus, the Coulombic interactions between the peptide and the membrane were calculated using the Gouy-Chapman theory that describes the electrostatic potential in the aqueous phase near the membrane. Peptide conformations and locations near the membrane, and changes in the membrane width, were sampled at random, using the Metropolis criterion, taking into

SUBMITTER: Shental-Bechor D 

PROVIDER: S-EPMC1959530 | biostudies-literature | 2007 Sep

REPOSITORIES: biostudies-literature