Issue 1, 2012
From the journal:

MedChemComm

Membrane disrupting antimicrobial peptide dendrimers with multiple amino termini†

Michaela Stach,a   Noélie Maillard,a   Rameshwar U. Kadam,a   David Kalbermatter,a   Marcel Meury,c   Malcolm G. P. Page,b   Dimitrios Fotiadis,c   Tamis Darbrea  and  Jean-Louis Reymond*a  

* Corresponding authors

a Department of Chemistry and Biochemistry, University of Berne, Freiestrasse 3, Berne, Switzerland
E-mail: jean-louis.reymond@ioc.unibe.ch
Fax: +41 31 631 80 57
Tel: +41 31 631 43 25

b Basilea Pharmaceutica Ltd., Grenzacherstrasse 487, PO Box, 4005 Basel, Switzerland

c Institute of Biochemistry and Molecular Medicine, University of Berne, Bühlstrasse 28, Berne, Switzerland

Abstract

Antimicrobial peptide dendrimer H1 Leu8(Lys-Leu)4(Lys-Phe)2Lys-LysNH2 (Lys = branching lysine) was identified by screening a 6750-membered combinatorial library by the bead-diffusion assay. Sequence variations also revealed dendrimer bH1 Leu8(Dap-Leu)4(Dap-Phe)2Dap-LysNH2 (Dap = branching 2,3-diaminopropanoic acid) as a more potent analog. H1 and bH1 showed good antimicrobial activities mediated by membrane disruption (MIC = 2–4 μg mL−1 on Bacillus subtilis and Escherichia coli) but low hemolytic activity (MHC = 310 μg mL−1 respectively >2000 μg mL−1).

Graphical abstract: Membrane disrupting antimicrobial peptide dendrimers with multiple amino termini

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Article information

DOI
https://doi.org/10.1039/C1MD00272D
Article type
Concise Article
Submitted
26 Oct 2011
Accepted
01 Nov 2011
First published
23 Nov 2011

Med. Chem. Commun., 2012,3, 86-89

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Membrane disrupting antimicrobial peptide dendrimers with multiple amino termini

M. Stach, N. Maillard, R. U. Kadam, D. Kalbermatter, M. Meury, M. G. P. Page, D. Fotiadis, T. Darbre and J. Reymond, Med. Chem. Commun., 2012, 3, 86 DOI: 10.1039/C1MD00272D

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