Tetrafibricin has a high selectivity for GPIIb/IIIa: comparison of the effects of tetrafibricin and RGDS on GPIIb/IIIa and the vitronectin receptor

Biochemical and Biophysical Research Communications
T SatohB Steiner

Abstract

The specificity of tetrafibricin was examined by comparing its activities on GPIIb/IIIa and on the vitronectin receptor (alpha v beta 3) with those of Arg-Gly-Asp-Ser (RGDS) on the same receptors. Tetrafibricin, which inhibited fibrinogen-GPIIb/IIIa binding 10 times more potently than RGDS, was three orders of magnitude less potent compared to RGDS on the inhibition of fibrinogen binding to alpha v beta 3. Furthermore, tetrafibricin potently inhibited platelet adhesion to both fibrinogen and von Willebrand factor. Whereas, there was no significant inhibition observed in the GPIIb/IIIa-independent cellular adhesions. These results suggest that tetrafibricin is highly selective for GPIIb/IIIa.

Citations

Jan 26, 2007·Organic Letters·Ricardo Lira, William R Roush
May 16, 2020·Natural Product Reports·Ryan M Friedrich, Gregory K Friestad
Jan 3, 2003·Organic Letters·Yoshihisa KobayashiYoshito Kishi
Mar 28, 2013·Journal of the American Chemical Society·Philippe Nuhant, William R Roush
Jan 16, 2014·Organic Letters·Takahiko ItohMichael J Krische

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