Identification of thrombin inhibiting antithrombin-III like protein from using approach and in vitro validation of thrombin inhibition activity in crude protein.

Thrombosis is characterized by the formation of clots in the blood vessels. Antithrombin-III deficiency in the blood causes thrombus formation. Supplementing antithrombin-III may serve as anticoagulant therapy. In the present studies, an antithrombin like Protein from has been identified and characterized using approach. Based on sequence homology, an ALPP was selected depending upon its highest binding affinity of -41.28 kcal/mol with thrombin. Thrombin structure complexed with ALPP was docked with TAME using AutoDock Vina. No binding was observed for TAME at Ser of thrombin. MD simulation (50 ns) was performed to evaluate the flexibility and stability of docked complexes. assays with crude protein showed 78% thrombin inhibition at 5 µg and calculated IC value was 0.188 µg. The presence of thrombin inhibitors in crude protein was also confirmed by reverse zymography. Thus, it is very likely that the protein identified from may act as thrombin inhibitor.