1197-18-8

Tranexamic acid (TXA) was invented by Japanese scientists Shosuke and Utako Okamoto shortly after World War II. TXA is an antifibrinolytic drug that reduces bleeding by inhibiting the enzymatic breakdown of fibrin blood clots. Plasminogen, a glycoprotein pro-enzyme produced in the liver, is converted into the fibrinolytic enzyme plasmin by tissue plasminogen activator (tPA). The plasminogen molecule is folder into loops called kringles that protrude like fingers. These fingers bind to fibrin via lysine-binding sites on their tips. If the lysine residues on fibrin are enzymatically removed, plasminogen binding is inhibited. Fibrin binds both plasminogen and tPA which localizes and promotes plasmin production. Plasmin that is bound to fibrin is shielded from plasmin inhibitors. Plasmin cuts fibrin into fibrin degradation products. This exposes more lysine molecules which bind more plasminogen, thus accelerating fibrinolysis. TXA has a molecular structure similar to lysine and inhibits fibrinolysis by inhibiting the binding of plasminogen to fibrin.

Among patients with bleeding trauma, the use of tranexamic acid, a fibrinolysis inhibitor, was associated with a significant reduction in overall mortality. Similar results have been reported in patients with traumatic brain injury and established obstetrical hemorrhage.

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InChI:InChI=1/C8H15NO2/c9-5-6-1-3-7(4-2-6)8(10)11/h6-7H,1-5,9H2,(H,10,11)/t6-,7-