Abstract
The process of blood coagulation is protecting organism from blood loss in case of surface injuries, and is ensuring blood circulation without formation of thrombus. The abnormal functioning of haemostasis is resulting in a many diseases in the recent years. Several serine proteinases and their inhibitors have a very important role in the process of the blood coagulation and are a strong potential alternative for the prevention and treatment of such illnesses. Herein, we report on anticoagulant activity, according to APTT of newly synthesized amide analogues of isoforms 2 and 3 of antistasin. Our study reveals that the replacement of carboxyl with amide function in a C-terminus of peptides is leading to significant increase of the anticoagulant activity. Additionally, some kinetic investigations on the same analogues are done. Our results show that both free acids and amides shortened analogues have a mixed type of inhibition related to serine proteinases from the blood coagulation cascade. The calculated Ki values for the model and the investigated serine proteinases show some selectivity of analogue Phe-Ile-Arg-Pro-Lys-Arg-NH2. The obtained kinetic data correlates with the anticoagulant activity of the newly synthesized analogues.
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Danalev, D., Marinkova, D., Raykova, R. et al. Kinetic Investigation and Anticoagulant Activity of Amide Analogues of Isoform 2 and 3 of Antistasin. Int J Pept Res Ther 20, 195–200 (2014). https://doi.org/10.1007/s10989-013-9381-9
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DOI: https://doi.org/10.1007/s10989-013-9381-9