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. 2007 Nov 20;46(46):13437-42.
doi: 10.1021/bi7015553. Epub 2007 Oct 18.

Enhanced membrane pore formation by multimeric/oligomeric antimicrobial peptides

Christopher J Arnusch  1 , Hilbert Branderhorst, Ben de Kruijff, Rob M J Liskamp, Eefjan Breukink, Roland J Pieters
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Enhanced membrane pore formation by multimeric/oligomeric antimicrobial peptides

Christopher J Arnusch et al. Biochemistry. .

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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