Issue 78, 2013
From the journal:

Chemical Communications

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  

* 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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Article information

DOI
https://doi.org/10.1039/C3CC44912B
Article type
Communication
Submitted
01 Jul 2013
Accepted
01 Aug 2013
First published
01 Aug 2013

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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