Non-peptidic phenyl-based thrombin inhibitors: exploring structural requirements of the S1 specificity pocket with amidines.
نویسندگان
چکیده
We expand the structural requirements and structure-activity relationship of a novel class of non-peptidic aryl-based thrombin inhibitors through exploration of the S1 specificity pocket of thrombin using flexible and constrained amidines. The most active compound of this class is 11 with Ki = 69 nM, which is ca. 15-fold less potent than constrained guanidine 5.
منابع مشابه
Chem. Pharm. Bull. 53(1) 22—26 (2005)
critical role in the blood coagulation cascade. Thrombin converts fibrinogen into fibrin which forms part of the blood clot, and activates other blood coagulation factors such as V, VIII, XIII, and protein C. Moreover, thrombin also activates blood platelets, and acts as a mitogen for various cell types. Thus, thrombin has become a special target in the design and development of antithrombotic ...
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عنوان ژورنال:
- Bioorganic & medicinal chemistry letters
دوره 10 1 شماره
صفحات -
تاریخ انتشار 2000