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Rapid Identification of Potent Nonpeptidic Serine Protease Inhibitors
Author(s) -
Salisbury Cleo M.,
Ellman Jonathan A.
Publication year - 2006
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200600081
Subject(s) - serine protease , proteases , serine , chemistry , enzyme , biochemistry , enzyme inhibitor , phosphonate , drug discovery , stereochemistry , protease , computational biology , biology
Substrate activity screening was used to rapidly identify a novel and potent ( k inact / K i =59 000 M −1 s −1 ) nonpeptidic chymotrypsin inhibitor with M W <500. The inhibitor is more potent than the best reported tetrapeptidyl phosphonate chymotrypsin inhibitor and demonstrated selectivity over a panel of other serine proteases, including the closely related enzyme cathepsin G.