Electrostatics and flexibility drive membrane recognition and early penetration by the antimicrobial peptide dendrimer bH1

Abstract

Molecular dynamics simulations of the polycationic antimicrobial peptide dendrimer bH1 (Leu)8(DapLeu)4(DapPhe)2DapLys-NH2 binding to membranes suggest that electrostatic interactions with the polyanionic lipopolysaccharide (LPS) and conformational flexibility of the 2,3-diaminopropanoic acid (Dap) branching units drive its selective insertion into microbial membranes. © 2013 The Royal Society of Chemistry.