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|Title:||Synthesis of 2-phenylisothiazol-3(2H)-one 1,1 dioxides: inhibitors of human leukocyte elastase.|
|Citation:||Zeitschrift fur Naturforschung Section B-A Journal of Chemical Sciences, 2003; 58b:111-120|
|Publisher:||Verlag Z Naturforsch|
|Michael Gutschow, Markus Pietsch, Kathleen Taubert, Tonia H. E. Freysoldt, and Barbel Schulze|
|Abstract:||A series of 2-phenylisothiazol-3(2H)-one 1,1-dioxides 14a – q were synthesized by oxidation of isothiazolium perchlorates 12. The inhibition of the serine proteases cathepsin G, chymotrypsin and human leukocyte elastase (HLE) by 14 was investigated. Some 4,5-diphenyl substituted derivatives ( 14i – k) were found to inhibit HLE in a time-dependent manner and exhibited kobs/[I] values > 500 M−1s−1. 14k (kobs/[I] = 2400 M−1s−1), was the most potent HLE inhibitor of this series. Kinetic investigations led to the conclusion that 2-phenylisothiazol-3(2H)-one 1,1-dioxides interact with HLE at the active site as well as at another binding site, resulting in a complex type of inhibition.|
|Keywords:||Sultams; Human Leukocyte Elastase; Enzyme Inhibition|
|Appears in Collections:||Chemistry publications|
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