Structure-Based design, synthesis and SAR of a novel series of thiopheneamidine urokinase plasminogen activator inhibitors

Article abstract of DOI:10.1016/S0960-894X(01)00247-5

The serine protease urokinase plasminogen activator (uPA) is thought to play a central role in tumor metastasis and angiogenesis. Molecular modeling studies suggest that 5-thiomethylthiopheneamidine inhibits uPA by binding at the S1 pocket of the active site. Further structure based elaboration of this residue resulted in a novel class of potent and selective inhibitors of uPA.