Design of Novel, Nonpeptidic Thrombin Inhibitors and Structure of a Thrombin–Inhibitor Complex

A strong inhibition of the serine protease thrombin, important in the blood coagulation process, was achieved through de novo designed inhibitors. The most active compound is shown. The X-ray crystal structure of the thrombin–inhibitor complex showed the binding mode of these compounds and confirmed that only the enantiomer predicted by computer modeling was bound in the active site.