Exploration of Active Site-Directed Plasmin Inhibitors: Beyond Tranexamic Acid

Plasmin (Plm), a trypsin-like serine protease, is responsible for fibrinolysis pathway and pathologic events, such as angiogenesis, tumor invasion, metastasis, alters the expression of cytokines. A growing body data indicates that Plm inhibitor potential candidate an anti-inflammatory anti-cancer agent. class active site-directed plasmin inhibitors containing tranexamic acid residue has been designed. As evidenced by docking studies, binds to site not lysine binding (LBS) in plasmin, thus preventing from digesting substrate. Further optimization series, concerning both activity selectivity, led second generation inhibitors. This review focuses on inhibitory activity-structure relationship with goal realizing their design clinical application.