PMID: 7519850Aug 1, 1994Paper

Tetrafibricin, a novel non-peptide fibrinogen receptor antagonist, induces conformational changes in glycoprotein IIb/IIIa

The Biochemical Journal
T SatohB Steiner

Abstract

Arg-Gly-Asp (RGD) is an amino acid sequence in fibrinogen recognized by platelet glycoprotein (GP) IIb/IIIa. Recently, it was found that RGD peptide binding to GPIIb/IIIa leads to conformational changes in the complex that are associated with the acquisition of high-affinity fibrinogen-binding function. In this study, we found that tetrafibricin, a novel non-peptidic GPIIb/IIIa antagonist, induced similar conformational changes in GPIIb/IIIa as did RGD peptides. Tetrafibricin increased the binding of purified inactive GPIIb/IIIa to immobilized pl-80, a monoclonal antibody that preferentially recognizes ligand-occupied GPIIb/IIIa. Exposure of the pl-80 epitope by tetrafibricin was also observed on resting human platelets by flow cytometry. On intact platelets, the conformational changes transformed GPIIb/IIIa into a high-affinity receptor for fibrinogen and triggered subsequent platelet aggregation. Tetrafibricin is the first non-peptidic GPIIb/IIIa antagonist reported that has the capacity to induce conformational changes in GPIIb/IIIa.

Citations

May 16, 2020·Natural Product Reports·Ryan M Friedrich, Gregory K Friestad
Jan 3, 2003·Organic Letters·Yoshihisa KobayashiYoshito Kishi
Oct 14, 2010·Organic Letters·Gregory K Friestad, Gopeekrishnan Sreenilayam
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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