Mechanism-based inhibitors of serine proteinases based on the Gabriel-Colman rearrangement

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Authors
Groutas, William C.
Chong, Lee S.
Venkataraman, Radhika
Epp, Jeffrey B.
Kuang, Rongze
Brubaker, Michael J.
Houser-Archield, Nadene
Huang, He
McClenahan, Jerald J.
Advisors
Issue Date
1993-08-16
Type
Article
Keywords
Research Support, U.S. Gov't, P.H.S.
Research Projects
Organizational Units
Journal Issue
Citation
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.

Table of Contents
Description
Full text of this article is not available in SOAR.
Publisher
Elsevier
Journal
Book Title
Series
Biochemical and biophysical research communications
Biochem. Biophys. Res. Commun.
PubMed ID
DOI
ISSN
0006-291X
EISSN