Development of MDL 28,050, a small stable antithrombin agent based on a functional domain of the leech protein, hirudin

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Title:	Development of MDL 28,050, a small stable antithrombin agent based on a functional domain of the leech protein, hirudin
Authors:	Krstenansky JL;Broersma RJ;Owen TJ;Payne MH;Yates MT;Mao SJT
Contributors:	Department of Biotechnology
Date:	1990-04
Issue Date:	2009-11-26 01:43:28 (UTC+0)
Publisher:	Asia University
Abstract:	MDL 28,050 is a decapeptide antithrombin agent that inhibits alpha-thrombin-induced fibrin clot formation by binding to a non-catalytic site on alpha-thrombin. It is the result of chemical and structural optimization of a functional domain of the leech anticoagulant, hirudin. In contrast to the contention that the polyanionic nature of this C-terminal functional domain governs its interaction with alpha-thrombin, systematic study of this region has shown the importance of the lipophilic residues for providing the functionality necessary for potent binding to alpha-thrombin. The development of MDL 28,050 and other effective antithrombin agents are outlined through the description of the structure-activity relationships (SAR) for these peptides. These peptides are effective in a variety of in vitro and in vivo models of thrombosis.
Relation:	Thrombosis and Haemostasis 63(2):208-14
Appears in Collections:	[Department of Biotechnology] Journal Article

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