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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 k obs /[I] values &gt; 500 M −1 s −1 . 14k (k obs /[I] = 2400 M −1 s −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.

Synthesis of 2-Phenylisothiazol-3(2H)-One 1,1-Dioxides: Inhibitors of Human Leukocyte Elastase