Enhanced membrane pore formation by multimeric/oligomeric antimicrobial peptides

Arnusch, C.J., Branderhorst, H., de Kruijff, B., Liskamp, R.M.J. , Breukink, E. and Pieters, R.J. (2007) Enhanced membrane pore formation by multimeric/oligomeric antimicrobial peptides. Biochemistry, 46(46), pp. 13437-13442. (doi:10.1021/bi7015553)

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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.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Liskamp, Professor Robert
Authors: Arnusch, C.J., Branderhorst, H., de Kruijff, B., Liskamp, R.M.J., Breukink, E., and Pieters, R.J.
College/School:College of Science and Engineering > School of Chemistry
Journal Name:Biochemistry
Publisher:American Chemical Society
ISSN:0006-2960
ISSN (Online):1520-4995

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