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  • Title: Inhibition of von Willebrand factor binding to platelets by two recognition site peptides: the pentadecapeptide of the carboxy terminus of the fibrinogen gamma chain and the tetrapeptide arg-gly-asp-ser.
    Author: Williams S, Gralnick H.
    Journal: Thromb Res; 1987 May 01; 46(3):457-71. PubMed ID: 3037722.
    Abstract:
    When platelets are stimulated by thrombin or ADP, von Willebrand factor (vWf) binds to the platelet glycoprotein IIb/IIIa (GPIIb/IIIa). Two recognition sites for vWf binding have been identified on the GPIIb/IIIa. One is a tetrapeptide, arg-gly-asp-ser (RGDS), and the second is a dodecapeptide with the sequence HHLGGAKQAGDV. We used these purified peptides to analyze the recognition specificities for the platelet binding of vWf. The RGDS and the pentadecapeptide totally inhibited 125I-vWf in a dose-dependent manner. The IC50 was 8 microM for the RGDS and 40 microM for the pentadecapeptide. These results indicate that the RGDS binds with higher affinity to a vWf binding site on GPIIb/IIIa than does the pentadecapeptide site. When the two peptides were incubated together, they augmented the inhibition of vWf binding. These data support the evidence that the GPIIb/IIIa has two distinct binding sites for vWf binding. The RGDS site appears to have a higher affinity for the vWf binding site than does the pentadecapeptide site.
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