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Issue 78, 2013
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Electrostatics and flexibility drive membrane recognition and early penetration by the antimicrobial peptide dendrimer bH1

Harish K. Ravi,a  Michaela Stach,a  Thereza A. Soares,b  Tamis Darbre,a  Jean-Louis Reymonda  and  Michele Cascella*a 
Author affiliations

* Corresponding authors

a Department of Chemistry and Biochemistry, University of Bern, Freiestrasse 3, 3012 Bern, Switzerland
E-mail: michele.cascella@iac.unibe.ch
Fax: +41 31 631 3994
Tel: +41 31 631 4256

b Department of Fundamental Chemistry, Federal University of Pernambuco, Av. Jornalista Anibal Fernandes, s/n° Cidade Universitária 50740-560, Recife, Brazil

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

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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
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    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

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