Jump to main content
Jump to site search

Issue 78, 2013
Previous Article Next Article

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

Author affiliations

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.

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

Back to tab navigation
Please wait while Download options loads

Supplementary files

Publication details

The article was received on 01 Jul 2013, accepted on 01 Aug 2013 and first published on 01 Aug 2013


Article type: Communication
DOI: 10.1039/C3CC44912B
Citation: Chem. Commun., 2013,49, 8821-8823
  •   Request permissions

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

    H. K. Ravi, M. Stach, T. A. Soares, T. Darbre, J. Reymond and M. Cascella, Chem. Commun., 2013, 49, 8821
    DOI: 10.1039/C3CC44912B

Search articles by author