Serendipitous discovery of an unexpected rearrangement leads to two new classes of potential protease inhibitors
Zhong, Jiaying Lai, Zhong Groutas, Christopher S. Wong, Tzutshin Gan, Xiangdong Alliston, Kevin R. Eichhorn, David M. Hoidal, John R. Groutas, William C.
Zhong, Jiaying
Lai, Zhong
Groutas, Christopher S.
Wong, Tzutshin
Gan, Xiangdong
Alliston, Kevin R.
Eichhorn, David M.
Hoidal, John R.
Groutas, William C.
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2004-12-01
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Article
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Research Support, Non-U.S. Gov't,Research Support, U.S. Gov't, P.H.S.
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Citation
Bioorganic & medicinal chemistry. 2004 Dec 1; 12(23): 6249-54.
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.
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Elsevier
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Bioorganic & medicinal chemistry
Bioorg. Med. Chem.
Bioorg. Med. Chem.
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0968-0896