Enhanced membrane pore formation by multimeric/oligomeric antimicrobial peptides

Christopher J. Arnusch, Hilbert Branderhorst, Ben De Kruijff, Rob M.J. Liskamp, Eefjan Breukink, Roland J. Pieters

Research output: Contribution to journalArticlepeer-review

75 Scopus citations

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.

Original languageEnglish
Pages (from-to)13437-13442
Number of pages6
JournalBiochemistry
Volume46
Issue number46
DOIs
StatePublished - 20 Nov 2007
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry

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