Novel Chromogenic Substrate for Bacterial β-Lactamases Based on Cephalosporin Modified with an Epoxy Group

Novel Chromogenic Substrate for Bacterial β-Lactamases Based on Cephalosporin Modified with an... Beta-lactamases are the key enzymes involved in resistance to beta-lactam antibiotics in pathogenic bacteria causing infectious diseases. The search for new inhibitors and the study of the resistance mechanisms require the production of chromogenic substrates for beta-lactamases. A novel cephalosporin derivative with an epoxy functional group named CMPD1 is synthesized. It is shown to be a substrate for TEM type beta-lactamases, which is hydrolyzed to form a colored product. The hydrolysis product has an optical absorption maximum at 450 nm. The difference in the absorption maxima of the substrate and the product is 95 nm, and, therefore, CMPD1 exceeds the previously described substrates, according to this parameter. It has been found that the CMPD1 compound is hydrolyzed only by the TEM type beta-lactamases that lack mutations in the active site. This can be used to study the mechanisms of the catalytic effect of beta-lactamases. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Moscow University Chemistry Bulletin Springer Journals

Novel Chromogenic Substrate for Bacterial β-Lactamases Based on Cephalosporin Modified with an Epoxy Group

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Publisher
Pleiades Publishing
Copyright
Copyright © 2018 by Allerton Press, Inc.
Subject
Chemistry; Chemistry/Food Science, general
ISSN
0027-1314
eISSN
1935-0260
D.O.I.
10.3103/S0027131418020086
Publisher site
See Article on Publisher Site

Abstract

Beta-lactamases are the key enzymes involved in resistance to beta-lactam antibiotics in pathogenic bacteria causing infectious diseases. The search for new inhibitors and the study of the resistance mechanisms require the production of chromogenic substrates for beta-lactamases. A novel cephalosporin derivative with an epoxy functional group named CMPD1 is synthesized. It is shown to be a substrate for TEM type beta-lactamases, which is hydrolyzed to form a colored product. The hydrolysis product has an optical absorption maximum at 450 nm. The difference in the absorption maxima of the substrate and the product is 95 nm, and, therefore, CMPD1 exceeds the previously described substrates, according to this parameter. It has been found that the CMPD1 compound is hydrolyzed only by the TEM type beta-lactamases that lack mutations in the active site. This can be used to study the mechanisms of the catalytic effect of beta-lactamases.

Journal

Moscow University Chemistry BulletinSpringer Journals

Published: May 30, 2018

References

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