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Because of its central role in the control of thrombus formation, the trypsin-like serine protease thrombin is an important target for therapeutic intervention in thrombotic disease. The patent literature from the past several years illustrates that the design of low molecular weight, active-site thrombin inhibitors has followed several major themes. These include tripeptides and peptide mimimics of the cleavage site of fibrinogen, analogues of tertiary arginine amides, and non-peptide inhibitors derived from screening and rational design. This report reviews the concurrent development of these approaches.
Wiley et al. (Sat,) studied this question.
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