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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

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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


Submitted
01 Jul 2013
Accepted
01 Aug 2013
First published
01 Aug 2013

Chem. Commun., 2013,49, 8821-8823
Article type
Communication

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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