Interactions of vancomycin and ristocetin with peptides as a model for protein binding
1984; Elsevier BV; Volume: 40; Issue: 3 Linguagem: Inglês
10.1016/0040-4020(84)85062-0
ISSN1464-5416
AutoresMichael P. Williamson, Dudley H. William, Stephen J. Hammond,
Tópico(s)Bacterial Genetics and Biotechnology
ResumoThe glycopeptide antibiotics vancomycin and ristocetin act by binding to peptides terminating in -D-Ala-D-Ala. Thermodynamic and kinetic parameters for the binding are evaluated and used in conjunction with previously determined stereochemical details to generate a complete picture of the binding interaction. A conformational change of the antibiotics is necessary to permit fast on-rates, and produces a hydrophobic pocket for the peptide carboxylate group. We discuss an unusual salt bridge and consider the origins of the high specificity of the antibiotics. The discussion is extended to macromolecule-substrate interactions. The importance of fast access to binding sites and complementarity of hydrogen bonding pairs is stressed.
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