Use of model cell membranes to demonstrate templated binding of vancomycin group antibiotics

Andrew C. Try, Gary J. Sharman, Robert J. Dancer, Ben Bardsley, R. M H Entress, Dudley H. Williams*

*Corresponding author for this work

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

In this paper we demonstrate the importance of binding geometry and dimerisation at the surface of model cell membranes in the mode of action of the clinically important glycopeptide antibiotics. This has been achieved through the use of model cell membranes (micelles and vesicles) to which cell wall analogues are anchored via a hydrophobic decanoyl chain. A number of -D-Ala-terminating cell wall analogues, ranging from two to six residues in length, have been used. Dipeptide, pentapeptide and hexapeptide display enhanced binding to the antibiotic at the model cell surface, but tripeptide and tetrapeptide do not. The possible implications of the observed binding geometries for bacterial systems are discussed.

Original languageEnglish
Pages (from-to)2911-2917
Number of pages7
JournalJournal of the Chemical Society - Perkin Transactions 1
Issue number19
Publication statusPublished - 7 Oct 1997

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