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Issue 1, 2012
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Membrane disrupting antimicrobial peptide dendrimers with multiple amino termini

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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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Publication details

The article was received on 26 Oct 2011, accepted on 01 Nov 2011 and first published on 23 Nov 2011


Article type: Concise Article
DOI: 10.1039/C1MD00272D
Citation: 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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