Mechanism-based inhibitors of serine proteinases based on the Gabriel-Colman rearrangement
Date
1993-08-16Author
Groutas, William C.
Chong, Lee S.
Venkataraman, Radhika
Epp, Jeffrey B.
Kuang, Rongze
Brubaker, Michael J.
Houser-Archield, Nadene
Huang, He
McClenahan, Jerald J.
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Biochemical and biophysical research communications. 1993 Aug 16; 194(3): 1491-9.
Abstract
Neutrophil-derived mediators such as, for example, the serine proteinase elastase, cathepsin G and proteinase 3, play a critical role in inflammatory lung disease. This report describes the design, synthesis and in vitro inhibitory activity of some novel mechanism-based inhibitors of human leukocyte elastase and cathepsin G. The design of the inhibitors is based on the Gabriel-Colman rearrangement. The behavior of the synthesized compounds toward elastase and cathepsin G with respect to inhibitory prowess, mode of interaction, specificity, etc., has been found to be dependent on the recognition and reactivity elements present in each inhibitor.
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