The Structure of Synthetic Oligosaccharides in Relation to Factor IXa Inhibition

Autor:	C. Gaich, Françoise Bono, J. M. Herbert, Petitou Maurice, Pierre-Alexandre Driguez, J. P. Hérault, P. Duchaussoy
Rok vydání:	2002
Předmět:	chemistry.chemical_classification Molecular mass Stereochemistry Antithrombin Biological activity Hematology Oligosaccharide Factor IXa Thrombin Enzyme Biochemistry chemistry medicine Structure–activity relationship medicine.drug
Zdroj:	Thrombosis and Haemostasis. 88:432-435
ISSN:	2567-689X 0340-6245
DOI:	10.1055/s-0037-1613234
Popis:	SummaryWe investigated the effect of various oligosaccharides (OS) on the inhibition of factor IXa by antithrombin (AT) in a purified system. The OS comprised the AT-binding pentasaccharide sequence prolonged by saccharide chains with various lengths and charges. We show that factor IXa inhibition depended on the molecular weight of the OS. Factor IXa was not inhibited by the AT-binding pentasaccharide alone, but was inhibited if it was prolonged by a sulphated dodecasaccharide at the non-reducing end. The overall charge was also important since factor IXa inhibition was negligible if the pentasaccharide was prolonged by a non-sulphated dodecasaccharide. Using compounds containing a non-sulphated spacer, we showed that the central part of the OS was not critical. This study therefore demonstrates that the minimal OS structure necessary for catalysing factor IXa inhibition by AT is close to that required for catalysing thrombin inhibition.
Databáze:	OpenAIRE
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