The synthesis and binding of N-terminal derivatives of vancomycin to a bacterial cell wall analogue

Thomas F. Gale, Jochen Görlitzer, Simon W. O'Brien, Dudley H. Williams

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)

Abstract

We report the synthesis of novel derivatives of the glycopeptide antibiotic vancomycin, modified at the N-terminus. Binding constants were measured for the association of these derivatives with the tripeptide analogue N,N-diacetyl-Llysyl-D-alanyl-D-alanine. Replacement of the sp3 centre of the leucine residue of vancomycin with an sp2 centre resulted in weaker binding in all cases. These findings contrast with the relatively strong binding of some of the analogous derivatives previously obtained from ristocetin A. The reduction in the binding affinities of the vancomycin derivatives is attributed to a conformational change in the antibiotic which is not possible in the analogous derivatives of the aglycone of ristocetin.

Original languageEnglish
Pages (from-to)2267-2270
Number of pages4
JournalJournal of the Chemical Society - Perkin Transactions 1
Issue number16
DOIs
Publication statusPublished - Jan 1 1999

ASJC Scopus subject areas

  • Chemistry(all)

Fingerprint Dive into the research topics of 'The synthesis and binding of N-terminal derivatives of vancomycin to a bacterial cell wall analogue'. Together they form a unique fingerprint.

Cite this