A peptide binding chromogenic assay for detecting glycopeptide antibiotics

A solid-phase peptide binding assay, based on the mechanism of action of glycopeptide antibiotics, was developed for detecting this chemical class of metabolites. Utilizing a pentapeptide (L-alanyl-D-isoglutaminyl-L-lysyl-D-alanine)-bovine serum albumin conjugate immobilized on the wall of microtite...

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Bibliographic Details
Published in:Journal of Industrial Microbiology 1989, Vol.4 (1), p.43-47
Main Authors: MAHONEY, D. F, BAISDEN, D. K, YAO, R. C
Format: Article
Language:English
Subjects:
Antibiotics
Biological and medical sciences
Biotechnology
Fundamental and applied biological sciences. Psychology
Health. Pharmaceutical industry
Industrial applications and implications. Economical aspects
Production of active biomolecules
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Summary:A solid-phase peptide binding assay, based on the mechanism of action of glycopeptide antibiotics, was developed for detecting this chemical class of metabolites. Utilizing a pentapeptide (L-alanyl-D-isoglutaminyl-L-lysyl-D-alanine)-bovine serum albumin conjugate immobilized on the wall of microtiter wells the binding of the vancomycin-alkaline phosphatase to the peptide could be demonstrated by subsequently monitoring the enzyme activity. The presence of glycopeptides in fermentation broths could be detected and quantified with a competitive binding assay. Peptides with a D-alanyl-D-alanine carboxyl terminus were necessary for the binding of these glycopeptides, thus confirming the mode of action of this class of antibiotics.
ISSN:0169-4146
1476-5535
DOI:10.1007/BF01569692