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J Med Chem ; 60(12): 5209-5215, 2017 06 22.
Article in English | MEDLINE | ID: mdl-28564542

ABSTRACT

Serine hydrolases are susceptible to potent reversible inhibition by boronic acids. Large collections of chemically diverse boronic acid fragments are commercially available because of their utility in coupling chemistry. We repurposed the approximately 650 boronic acid reagents in our collection as a directed fragment library targeting serine hydrolases and related enzymes. Highly efficient hits (LE > 0.6) often result. The utility of the approach is illustrated with the results against autotaxin, a phospholipase implicated in cardiovascular disease.


Subject(s)
Boronic Acids/chemistry , Phosphoric Diester Hydrolases/metabolism , Serine Proteinase Inhibitors/pharmacology , Small Molecule Libraries/pharmacology , Structure-Activity Relationship , Crystallography, X-Ray , Drug Evaluation, Preclinical/methods , Humans , Nitriles/chemistry , Phosphoric Diester Hydrolases/chemistry , Phosphoric Diester Hydrolases/genetics , Serine Endopeptidases/metabolism , Serine Proteinase Inhibitors/chemistry , Small Molecule Libraries/chemistry , Surface Plasmon Resonance
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