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Enhanced membrane pore information by multimeric/oligomeric antimicrobial peptides

Authors :
Arnusch, C.J.
Branderhorst, H.M.
de Kruijff, B.
Liskamp, R.M.J.
Breukink, E.J.
Pieters, R.J.
Biochemie van Membranen
Chemical Biology & Organic Chemistry
Medicinal Chemistry
SYNTHESE
Dep Farmaceutische wetenschappen
Dep Scheikunde
Publication Year :
2007

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 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.

Details

Database :
OpenAIRE
Accession number :
edsair.od.......101..eb247117ee86217ef180fbd7cc2343cf