Anticoagulant peptides: nature of the interaction of the C-terminal region of hirudin with a noncatalytic binding site on thrombin

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题名:	Anticoagulant peptides: nature of the interaction of the C-terminal region of hirudin with a noncatalytic binding site on thrombin
作者:	Krstenansky JL;Owen TJ;Yates MT;Mao SJT
贡献者:	Department of Biotechnology
日期:	1987-09
上传时间:	2009-11-26 01:43:31 (UTC+0)
出版者:	Asia University
摘要:	A series of 20 C-terminal fragment analogues of the anticoagulant peptide hirudin were synthesized by solid-phase techniques in order to investigate the nature of the thrombin-hirudin interaction. Inhibition of plasma fibrin clot formation by thrombin in vitro was used as a measure of anticoagulant activity. In the minimum region necessary for detectable anticoagulant activity, hirudin56-64, positions Phe56, Glu57, Ile59, Pro60, and Leu64 are sensitive to modification. These residues are apparently important for direct interaction with thrombin or for maintaining a favorable conformation for the interaction. On the basis of conformational analysis of this region by computational methods, a "kinked" amphipathic alpha-helical structure, which orients all of the residues most critical for activity on one face of the helix, is proposed.
關聯:	Journal of Medicinal Chemistry 30(9):1688-91
显示于类别:	[生物科技學系] 期刊論文

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