Mimetics of the Arg-Gly-Asp Sequence: Synthesis and Studies of the Antiaggregative Properties.

Autor:	Gribovskaya, O. V., Martinovich, V. P., Rodko, E. V., Rasyuk, E. D., Ryabtseva, T. V., Golubovich, V. P.
Předmět:	FIBRINOGEN BINDING sites BLOOD platelets PEPTIDE synthesis
Zdroj:	Russian Journal of Bioorganic Chemistry; Nov2021, Vol. 47 Issue 6, p1249-1256, 8p
Abstrakt:	It is known that the Arg-Gly-Asp sequence in the fibrinogen molecule is key in binding to the receptors on the surface of platelets. We searched for the compounds which were able to inhibit the binding and synthesized the following analogs of this sequence: 2-acetoxybenzoyl-Arg-βAla-Asp, 4-piperidinecarbonyl-βAla-Asp, and 4-aminobezoyl-βAla-Asp. These compounds were shown to inhibit the platelets aggregation in a different degree. The 2-acetoxybenzoyl-Arg-βAla-Asp analog demonstrated the highest inhibitory activity. A decrease in the expression of the CD62p and CD63 markers on platelets was also found after the action of the Arg-Gly-Asp analogs, confirming the ability of these compounds to block the fibrinogen binding sites for the GP IIb/IIIa glycoprotein receptors. [ABSTRACT FROM AUTHOR]
Databáze:	Complementary Index
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