Synthesis and study on a novel inhibitor of thrombin containing no side chain at the P1 position of the polypeptide chain.
The presented work allows one to speculate that the hydrophobic contacts of the residues located at the P2 and P3 positions with the corresponding subsites of thrombin (S2 and S3) allow the synthesis of compounds that can react with thrombin specifically and probably may not interact with other trypsin-like serine proteases. Substitution of proline by m-Abz-residue may result in the development of novel substrates and inhibitors for thrombin.
Gershkovich
A A
AA
Institute of Bioorganic Chemistry and Petrochemistry, National Academy of Sciences of the Ukraine, Kiev, Ukraine.
Kara
D I
DI
Kibirev
V K
VK
D000818:Animals; D000991:Antithrombins / Q000138:chemical synthesis* / Q000737:chemistry; D006801:Humans; D013917:Thrombin / Q000037:antagonists & inhibitors*
D000991:Antithrombins; D013917:Thrombin