Electrostatics and Flexibility Drive Membrane Recognition and Early Penetration by Antimicrobial Peptide Dendrimer bH1

August 1, 2013

Journal Article

Electrostatics and Flexibility Drive Membrane Recognition and Early Penetration by Antimicrobial Peptide Dendrimer bH1

Abstract

Molecular dynamics simulation of polycationic antimicrobial peptide dendrimer bH1 (Leu)8(DapLeu)4(DapPhe)2DapLys- NH2 binding to membranes suggest that electrostatic 10 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.

Revised: October 23, 2013 | Published: August 1, 2013

Citation

Ravi H., M. Stach, T.A. Soares, T. Darbre, J. Reymond, and M. Cascella. 2013. Electrostatics and Flexibility Drive Membrane Recognition and Early Penetration by Antimicrobial Peptide Dendrimer bH1. Chemical Communications 49, no. 78:8821-8823. doi:10.1039/C3CC44912B