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.
|Number of pages||7|
|Journal||Journal of the Chemical Society - Perkin Transactions 1|
|Publication status||Published - 7 Oct 1997|