The stabilization of vancomycin by peptidoglycan analogs.
- 1 January 1985
- journal article
- research article
- Published by Japan Antibiotics Research Association in The Journal of Antibiotics
- Vol. 38 (1) , 51-57
- https://doi.org/10.7164/antibiotics.38.51
Abstract
The glycopeptide antibiotic vancomycin is unstable in solution. It undergoes a rearrangement involving the conversion of an asparagine residue to isoaspartate to give an antibiotically inactive species, CDP-I. Peptide analogs of bacterial peptidoglycan, such as Ac-D-Ala-D-Ala and di-Ac-L-Lys-D-Ala-D-Ala bind to vancomycin and stabilize the antibiotic against degradation and consequent loss of activity. Protection by peptide is effective even under prolonged heating at 80.degree. C or steam sterilization (30 min, 104 kg/m2).This publication has 8 references indexed in Scilit:
- Interactions of vancomycin and ristocetin with peptides as a model for protein bindingTetrahedron, 1984
- Vancomycin: structure and transformation to CDP-IJournal of the American Chemical Society, 1983
- Detailed binding sites of the antibiotics vancomycin and ristocetin A: determination of intermolecular distances in antibiotic/substrate complexes by use of the time-dependent NOEJournal of the American Chemical Society, 1983
- Structure revision of the antibiotic vancomycin. Use of nuclear Overhauser effect difference spectroscopyJournal of the American Chemical Society, 1981
- Binding site of the antibiotic vancomycin for a cell-wall peptide analogJournal of the American Chemical Society, 1981
- Comparison of a radioimmunoassay and a microbiological assay for measurement of serum vancomycin concentrationsAntimicrobial Agents and Chemotherapy, 1980
- Structure of vancomycin and its complex with acetyl-D-alanyl-D-alanineNature, 1978
- Studies on the Mechanism of Ristocetin-Induced Platelet AgglutinationJournal of Clinical Investigation, 1977