Journal
ANALYTICAL BIOCHEMISTRY
Volume 396, Issue 1, Pages 164-166Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.ab.2009.09.004
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Funding
- NIGMS NIH HHS [R01 GM060149, GM60149, R01 GM060149-05] Funding Source: Medline
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM060149] Funding Source: NIH RePORTER
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High-molecular-mass penicillin-binding proteins (HMM PBPs) are essential for bacterial cell wall biosynthesis and are the lethal targets of beta-lactam antibiotics. When purified, HMM PBPs give undetectable or weak enzyme activity. This has impeded efforts to develop assays for HMM PBPs and to develop new inhibitors for HMM PBPs as HMM PBP targeted antibacterial agents. However, even when purified, HMM PBPs retain their ability to bind beta-lactams. Here we describe a fluorescently detected microtiter plate-based assay for inhibitor binding to HMM PBPs based on competition with biotin-ampicillin conjugate (BIO-AMP) binding. (C) 2009 Elsevier Inc. All rights reserved.
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