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

作者信息

Zhong Jiaying, Lai Zhong, Groutas Christopher S, Wong Tzutshin, Gan Xiangdong, Alliston Kevin R, Eichhorn David, Hoidal John R, Groutas William C

机构信息

Department of Chemistry, Wichita State University, Wichita, KS 67260, USA.

出版信息

Bioorg Med Chem. 2004 Dec 1;12(23):6249-54. doi: 10.1016/j.bmc.2004.08.044.

DOI:10.1016/j.bmc.2004.08.044
PMID:15519167
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.

摘要

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