Inhibition of integrin-mediated platelet aggregation, fibrinogen-binding, and interactions with extracellular matrix by nonpeptidic mimetics of Arg-Gly-Asp.

@article{Varon1993InhibitionOI,
  title={Inhibition of integrin-mediated platelet aggregation, fibrinogen-binding, and interactions with extracellular matrix by nonpeptidic mimetics of Arg-Gly-Asp.},
  author={David Varon and Ofer Lider and Rima Dardik and Boris Shenkman and Ronen Alon and Rami Hershkoviz and G M Kapustina and Naphtali Savion and Uri Martinowitz and N Greenspoon},
  journal={Thrombosis and haemostasis},
  year={1993},
  volume={70 6},
  pages={1030-6}
}
The interaction of the activated platelet integrin, glycoprotein IIb-IIIa (GPIIb-IIIa) with fibrinogen and von-Willebrand factor (vWF) is essential for platelet aggregation. The minimal structure required for this integrin's binding to fibrinogen is the Arg-Gly-Asp (RGD) sequence. Inasmuch as normal level of GPIIb-IIIa-RGD interactions are required for… CONTINUE READING