Batroxobin
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Batroxobin is a defibrinogenating hemostatic agent derived from the venom of a pit viper, Bothrops atrox moojeni. In addition to batroxobin, the venom of Bothrops atrox has a composition of 10.2% neutral carbohydrate. Batroxobin is a serine protease, which cleaves the 16 Arginine - 17 Glycine bond in fibrinogen. The MW of batroxobin is approximately 43,000 g/mol-1, and it contains 231 amino acids. Batroxobin is inactivated by alpha2-macroglobulin, but not anti-thrombin compounds. Batroxobin will also bind fibrinogen in a manner different than thrombin and with a higher affinity. Once bound to fibrin, it will cause fibrin accretion(clot formation) to a degree 18 folds greater than thrombin. Currently use is experimental but trials have been conducted which support certain clinical applications. Recombinant Batroxobin in relatively affordable and could be accessed by mass production.
Batroxobin is a defibrinogenating hemostatic agent derived from the venom of a pit viper, Bothrops atrox moojeni. In addition to batroxobin, the venom of Bothrops atrox has a composition of 10.2% neutral carbohydrate. Batroxobin is a serine protease, which cleaves the 16 Arginine - 17 Glycine bond in fibrinogen. The MW of batroxobin is approximately 43,000 g/mol-1, and it contains 231 amino acids. Batroxobin is inactivated by alpha2-macroglobulin, but not anti-thrombin compounds. Batroxobin will also bind fibrinogen in a manner different than thrombin and with a higher affinity. Once bound to fibrin, it will cause fibrin accretion(clot formation) to a degree 18 folds greater than thrombin. Currently use is experimental but trials have been conducted which support certain clinical applications. Recombinant Batroxobin in relatively affordable and could be accessed by mass production.
Batroxobin is a thrombin like serine protease enzyme that will cleave fibrinogen. Cleavage at the16 Arginine - 17 Glycine bond in the A alpha chain of fibrinogen releases fibrinopeptide A and forms a fibrin I monomer that will spontaneously aggregate into a clot. The reduction of plasma fibrinogen by formation of fibrin microclots that are easily cleared by the reticuloendothelial system can decrease high blood viscosity which contributes to the formation of thromboemboli. In addition, batroxobin is reported to induce fibrinolysis by inducing the endothelial release of tissue plasminogen activator (tPA) from vascular endothelial cells. This effect may potentially be dose dependant.
No approved indications. Batroxobin is a defibrongenating agent which has been observed to reduce fibrinogen levels and thus reduce clot risk when used intravenously.
