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Enhanced membrane pore information by multimeric/oligomeric antimicrobial peptides

By C.J. Arnusch, H.M. Branderhorst, B. de Kruijff, R.M.J. Liskamp, E.J. Breukink and R.J. Pieters


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 poreforming 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

Year: 2007
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