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

Harish K. Ravi; Michaela Stach; Thereza A. Soares; Tamis Darbre; Jean-Louis Reymond; Michele Cascella

doi:10.1039/C3CC44912B

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 Reymond^a 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.

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

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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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Chemical Communications

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

Abstract

Supplementary files

Publication details

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

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