Literature DB >> 17944489

Enhanced membrane pore formation by multimeric/oligomeric antimicrobial peptides.

Christopher J Arnusch1, Hilbert Branderhorst, Ben de Kruijff, Rob M J Liskamp, Eefjan Breukink, Roland J Pieters.   

Abstract

The pore-forming antibacterial peptide magainin 2 was made divalent, tetravalent, and octavalent via a copper(I)-mediated 1-3 dipolar cycloaddition reaction ("click" chemistry). This series of pore-forming compounds was tested in vitro for their ability to form pores in large unilamillar vesicles (LUVs). A large increase in the pore-forming capability was especially observed with the tetravalent and octavalent magainin compounds in the LUVs consisting of DOPC, and the octavalent magainin compound showed a marked increase with the DOPC/DOPG LUVs. Activity was observed in the low nanomolar range for these compounds.

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Year:  2007        PMID: 17944489     DOI: 10.1021/bi7015553

Source DB:  PubMed          Journal:  Biochemistry        ISSN: 0006-2960            Impact factor:   3.162


  19 in total

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