ArticleMethods in molecular biology (Clifton, N.J.)2025
Microplate-Based Enzymatic Activity Assay Protocol Powered by Activity-Based Probes.
Article in Methods in molecular biology (Clifton, N.J.), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Fragment-based drug discovery: A graphical review.Current research in pharmacology and drug discovery · 2025Review
- Activity-based chemoproteomic profiling reveals the active kinome ofFrontiers in pharmacology · 2025Article
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Authors and funding
4 authors.
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Abstract
Identifying new enzymes and gaining insights into their mode of action (and inhibition) is a critical step in drug discovery. In this chapter, we describe a novel methodology that accelerates this process by combining the precision of activity-based protein profiling (ABPP) with the efficiency of microplate assay technology. Central to this approach is the use of competitive ABPP, which utilizes an activity-based probe (ABP) to directly observe and characterize the interactions between inhibitors and an enzyme. In this study, we use an in-house fluorophosphonate (FP)-based probe, as an example of an electrophilic probe, and pig liver esterase (PLE), as a model enzyme. Simple chemical modification of PLE to introduce a streptavidin tag enables its immobilization and presentation on a biotinylated assay plate. Subsequent competitive ABPP experiments using FP probes and a commercially derived compound library can be run in parallel. This setup allows for the identification of new inhibitors and the estimation of IC
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