Serendipitous discovery of an unexpected rearrangement leads to two new classes of potential protease inhibitors

No Thumbnail Available
Authors
Zhong, Jiaying
Lai, Zhong
Groutas, Christopher S.
Wong, Tzutshin
Gan, Xiangdong
Alliston, Kevin R.
Eichhorn, David M.
Hoidal, John R.
Groutas, William C.
Issue Date
2004-12-01
Type
Article
Language
eng
Keywords
Research Support, Non-U.S. Gov't , Research Support, U.S. Gov't, P.H.S.
Research Projects
Organizational Units
Journal Issue
Alternative Title
Abstract

The pathogenesis of a range of human diseases arises from the aberrant activity of proteolytic enzymes. Agents capable of selectively modulating the activity of these enzymes are of potential therapeutic value. Thus, there is a continuing need for the design of scaffolds that can be used in the development of new classes of protease inhibitors. We describe herein the serendipitous discovery of an unexpected rearrangement that leads to the formation of two novel templates that can be used in the design of protease inhibitors.

Description
Click on the DOI link below to access the article (may not be free).
Citation
Bioorganic & medicinal chemistry. 2004 Dec 1; 12(23): 6249-54.
Publisher
Elsevier
License
Journal
Volume
Issue
PubMed ID
DOI
ISSN
0968-0896
EISSN