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

— 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-piper...

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Bibliographic Details
Published in:Russian journal of bioorganic chemistry 2021-11, Vol.47 (6), p.1249-1256
Main Authors: Gribovskaya, O. V., Martinovich, V. P., Rodko, E. V., Rasyuk, E. D., Ryabtseva, T. V., Golubovich, V. P.
Format: Article
Language:English
Subjects:
Analogs
Binding sites
Biochemistry
Biomedical and Life Sciences
Biomedicine
Bioorganic Chemistry
Fibrinogen
Glycoproteins
Life Sciences
Organic Chemistry
Platelets
Receptors
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Summary:— 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.
ISSN:1068-1620
1608-330X
DOI:10.1134/S106816202106008X