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Type: Journal article
Title: Synthesis of 2-phenylisothiazol-3(2H)-one 1,1 dioxides: inhibitors of human leukocyte elastase.
Author: Gutschow, M.
Pietsch, M.
Taubert, K.
Freysoldt, T.
Schulze, B.
Citation: Zeitschrift fuer Naturforschung, Section B: A Journal of Chemical Sciences, 2003; 58b:111-120
Publisher: Verlag Z Naturforsch
Issue Date: 2003
ISSN: 0932-0776
Statement of
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
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Chemistry publications

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