ArticleAnalytical biochemistry2010
A microtiter plate-based beta-lactam binding assay for inhibitors of high-molecular-mass penicillin-binding proteins.
Article in Analytical biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 11 citations in OpenAlex.
- Chemical genetic approaches for the discovery of bacterial cell wall inhibitors.RSC medicinal chemistry · 2023Review
- Evaluation of the antibacterial activity of patchouli oil.Iranian journal of pharmaceutical research : IJPR · 2013Article
- Development of new drugs for an old target: the penicillin binding proteins.Molecules (Basel, Switzerland) · 2012Review
- Microtiter plate-based assay for inhibitors of penicillin-binding protein 2a from methicillin-resistant Staphylococcus aureus.Antimicrobial agents and chemotherapy · 2011Article
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
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.
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