Antimicrobial peptides are an abundant and diverse group of molecules that are produced
by many tissues and cell types in a variety of invertebrate, plant and animal species. Their …

Antimicrobial peptides (AMPs) have been isolated and characterized from tissues and
organisms representing virtually every kingdom and phylum. Their amino acid composition …

Recently we have shown that the free energy for pore formation induced by antimicrobial
peptides contains a term representing peptide-peptide interactions mediated by membrane …

Background The antibacterial activity of host defense peptides (HDP) is largely mediated by
permeabilization of bacterial membranes. The lipid membrane of enveloped viruses might …

As the number of membrane proteins in the Protein Data Bank increases, efforts to
understand how they interact with their natural environment are increasing in importance. A …

Many biological processes occur at the interface region of the cell—the cellular membrane.
The interaction of peptides with membranes is of great importance for the understanding of …

An 18-residue peptide, KWGAKIKIGAKIKIGAKI-NH2 was designed to form amphiphilic β-
sheet structures when bound to lipid bilayers. The peptide possesses high antimicrobial …

We report long time scale simulations of the 18-residue helical antimicrobial peptide
ovispirin-1 and its analogs novispirin-G10 and novispirin-T7 in SDS micelles. The SDS …

The membrane disruption mechanism of pandinin 1 (pin1), an antimicrobial peptide isolated
from the venom of the African scorpion, was studied using 31 P, 13 C, 1 H solid-state and …

We have carried out a 40-ns all-atom molecular dynamics simulation of the helical
antimicrobial peptide ovispirin-1 (OVIS) in a zwitterionic diphosphocholine (DPC) micelle …