Enhanced membrane pore formation by multimeric/oligomeric antimicrobial peptides
Publication date
2007-11-20
Authors
Arnusch, Christopher J.
Branderhorst, Hilbert
de Kruijff, B.
Liskamp, Rob
Breukink, Eefjan
Pieters, Roland J.
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Document Type
Article
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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. © 2007 American Chemical Society.
Keywords
copper ion, polypeptide antibiotic agent, article, channel gating, cycloaddition, in vitro study, priority journal
Citation
Arnusch, C J, Branderhorst, H, De Kruijff, B, Liskamp, R M J, Breukink, E & Pieters, R J 2007, 'Enhanced membrane pore formation by multimeric/oligomeric antimicrobial peptides', Biochemistry, vol. 46, no. 46, pp. 13437-13442. https://doi.org/10.1021/bi7015553