Thrombin is a trypsin-like serine protease that is encoded by the F2 gene in humans. Thrombin is produced by the enzymatic cleavage of two sites on prothrombin by activated Factor X (Xa). Thrombin in turn acts as a serine protease that converts soluble
Prothrombin (coagulationfactor II) is produced in the liver and is post-translationally modified in a vitamin K-dependent reaction that converts ten glutamic acids on prothrombin into gamma-carboxyglutamic acid. Prothrombin is proteolytically cleaved to
YM-75466 is a factor Xa inhibitor. YM-75466 did not prolong coagulation time even at the dose which exerted significant antithrombotic effects, while it decreased TAT level in plasma in a dose-dependent manner.
Milvexian, also known as BMS-986177 and JNJ-70033093, is a blood coagulationfactor XIa inhibitor. Milvexian demonstrated good selectivity over plasma kallikreinKi = 44 nM (400-fold selective), and chymotrypsinKi = 35 nM (318-fold selective). At a dose of 1.5 mg kg, Milvexian exhibited an overall exposure of 1215 nM h, low clearance of 10.3 mL min kg, and oral bioavailability of 32%.