biostudies-literatureLiu XNIGMS NIH HHS2082-93https://www.ebi.ac.uk/biostudies/studies/S-EPMC3777423biostudies-literatureUnknown13(14)The serine hydrolases constitute a large class of enzymes that play important roles in physiology. There is great interest in the development of potent and selective pharmacological inhibitors of these proteins. Traditional active-site inhibitors often have limited selectivity within this superfamily and are tedious and expensive to discover. Using the serine hydrolase RBBP9 as a model target, we designed a rapid and relatively inexpensive route to highly selective peptoid-based inhibitors that can be activated by visible light. This technology provides rapid access to photo-activated tool compounds capable of selectively blocking the function of particular serine hydrolases.Chembiochem : a European journal of chemical biologyRapid development of a potent photo-triggered inhibitor of the serine hydrolase RBBP9.PMC3777423R01 GM090294Liu XCravatt BFBachovchin DAKodadek TJSpeers AEDix MZuhl AMfalseRapid development of a potent photo-triggered inhibitor of the serine hydrolase RBBP9.The serine hydrolases constitute a large class of enzymes that play important roles in physiology. There is great interest in the development of potent and selective pharmacological inhibitors of these proteins. Traditional active-site inhibitors often have limited selectivity within this superfamily and are tedious and expensive to discover. Using the serine hydrolase RBBP9 as a model target, we designed a rapid and relatively inexpensive route to highly selective peptoid-based inhibitors that can be activated by visible light. This technology provides rapid access to photo-activated tool compounds capable of selectively blocking the function of particular serine hydrolases.2012-01-01T00:00:00Z2012 Sep2025-04-25T23:05:28.439Z2019-03-27T01:16:13ZS-EPMC37774232290780210.1002/cbic.201200445