Lipid-mediated synergistic interactions of antimicrobial peptides in membranes

Abstract

Biophysical and structural studies have shown that peptides interact with the membranes in a highly dynamic manner. Both peptides and lipids change and mutually adapt their conformation, membrane penetration and detailed morphology locally and globally forming supramolecular assemblies of variable shape and dimension. Charged amphipathic sequences such as antimicrobial and cell penetrating peptides tend to stay intercalated at the membrane interface. Although the membranes are soft and can adapt, at increasing peptide density they cause pronounced disruptions of the phospholipid bilayer packing.