Probing the disparate effects of arginine and lysine residues on antimicrobial peptide/bilayer association.

ABSTRACT: Antimicrobial peptides (AMPs) are key components of the innate immune response and represent promising templates for the development of broad-spectrum alternatives to conventional antibiotics. Most AMPs are short, cationic peptides that interact more strongly with negatively charged prokaryotic membranes than net neutral eukaryotic ones. Both AMPs and synthetic analogues with arginine-like side chains are more active against bacteria than those with lysine-like amine groups, though the atomistic mechanism for this increase in potency remains unclear. To examine this, we conducted comparative molecular dynamics simulations of a model negatively-charged membrane system interacting with two mutants of the AMP KR-12: one with lysine residues mutated to arginines (R-KR12) and one with arginine

SUBMITTER: Rice A 

PROVIDER: S-EPMC5582999 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature