Add time:08/11/2019 Source:sciencedirect.com
Synthetic peptides cyclized via disulfide linkages have been synthesized as conformationally restricted analogs of a novel class of antithrombotic peptides that inhibit fibrinogen cleavage by binding to a non-enzymatic site on thrombin. Several conformational models for these inhibitors have been considered and cyclic analogs were synthesized to test their validity. Compounds designed on an α-helical model yielded several cyclic anallogs that retained antithrombin activity. [d-Cys58, Cys61]-hirudin54–65, 5, and [d-Cys60, Cys63]-hirudin54–65, 6, had IC50 values of 26 and 30 μM, respectively, in an in vitro clot assay compared with a value of 3.7 μM for the linear hirudin54–65.
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