Poyarkov O. Novel thrombin inhibitors, their efficiency and selectivity of action

Thrombin is a plasma serine protease that plays a key role in coagulation. Investigation of novel inhibitors of thrombin, modified by different aromatic and heterocyclic and aliphatic moieties, and revealing of their structurally functional features of interaction with thrombin. Chemical synthesis, ЯМР-spectroscopy, LDI weight - spectrometry, the element analysis, tin lair and a liquid chromatography of low pressure and HPLC, enzymatic kinetics, MALDI ToF weight - spectrometry. The new class effective and high selective inhibitors of thrombin - lipo-retro-D-peptides is synthesized, some from them have shown selectivity to thrombin more than in 5000 times at micro molar values Ki. For the first time it is proved, that N a- Lauroyl arginine ethyl ester is competitive convertible inhibitors of thrombin and shows effectors action on plasmin and protease Dengue NS2 a virus of a tropical fever. For the first time method MALDI ToF MS has been used for research of structural features intact fibers. Sphere of use - bioorganic chemistry.