Interactions of the antimicrobial β-peptide β-17 with phospholipid vesicles differ from membrane interactions of magainins

Abstract

We have studied the interaction of β-17, a potent synthetic antimicrobial β-peptide, with phospholipids. We find that unlike other antimicrobial peptides such as magainin II, β-17 facilitates the formation of nonbilayer phases, indicating that the peptide promotes negative curvature. Studies of liposomal leakage also indicate a different mode of membrane interaction relative to magainin II, but both leakage and membrane binding show that β-17, like magainin II, has strong affinity for membranes containing anionic lipids. This is likely to be an important factor contributing to the antimicrobial specificity of the β-peptide.