Physical basis for membrane-charge selectivity of cationic antimicrobial peptides.
Antimicrobial peptides are known to selectively disrupt (highly charged) microbial membranes by asymmetrical incorporation into the outer layers. We present a physical basis for membrane-charge selectivity of cationic antimicrobial peptides. In particular, we provide a clear picture of how peptide-charge Q influences the asymmetrical insertion--one salient feature is the existence of an optimal peptide charge, at which selective insertion is optimized. Our results suggest that large Q is required for antimicrobial selectivity, consistent with experiments.
Taheri-Araghi
Sattar
S
Department of Physics and Astronomy, University of Waterloo, Waterloo, Ontario N2L 3G1, Canada.
Ha
Bae-Yeun
BY
D023181:Antimicrobial Cationic Peptides / Q000737:chemistry*; D002462:Cell Membrane / Q000737:chemistry*; D003198:Computer Simulation; D008051:Lipid Bilayers / Q000737:chemistry*; D008956:Models, Chemical; D008958:Models, Molecular; D010743:Phospholipids / Q000737:chemistry*; D055672:Static Electricity
D023181:Antimicrobial Cationic Peptides; D008051:Lipid Bilayers; D010743:Phospholipids