The structure-antiaggregative activity relationship in a series of Arg-Gly-Asp analogues

Autor:	O. V. Mel’nik, V. P. Golubovich, V. P. Martinovich
Rok vydání:	2006
Předmět:	Oligopeptide Stereochemistry Organic Chemistry Tripeptide Biochemistry chemistry.chemical_compound Protein structure chemistry Peptide synthesis Platelet aggregation inhibitor Structure–activity relationship Receptor Guanidine
Zdroj:	Russian Journal of Bioorganic Chemistry. 32:122-128
ISSN:	1573-9163 1068-1620
Popis:	A series of analogues of Arg-Gly-Asp tripeptide, the common structural element of most of the integrin receptor ligands, possessing different conformational features for the interaction with platelet receptors, were synthesized by the methods of conventional peptide chemistry for use in the search for antithrombotic agents. The distance between the guanidine group of Arg and the beta-carboxyl group of Asp was shown to affect the antiaggregative activity. A potent inhibitor of platelet aggregation, tripeptide Arg-betaAla-Asp, with IC50 = 10.6 microM (ADP, 1.5 microM), was revealed.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::a55829adc645825af0a6d9675a9e7998 https://doi.org/10.1134/s1068162006020038 Zobrazit plný text záznamu Full text from SpringerLink