von Willebrand factor – Glycoprotein Ib alpha interface (vWF-GPIbα interface)

The interface between von Willebrand factor (vWF) and the Glycoprotein Ib alpha (GPIbα) subunit of the platelet GPIb-IX-V complex is a critical mediator of primary hemostasis. This interaction is particularly vital under high-shear stress conditions, such as those found in narrowed arteries, where it facilitates the initial tethering and rolling of platelets on the exposed subendothelial matrix (UniProt P07359). In the context of adipose-derived platelets—platelets generated ex vivo from adipose-derived mesenchymal stem cells—the integrity and functionality of this interface are paramount for ensuring that these manufactured cells can effectively contribute to clot formation upon transfusion (Tobe et al., 2011). Therapeutically, targeting this interface with biologics like nanobodies or aptamers provides a potent strategy for preventing arterial thrombosis and treating conditions like thrombotic thrombocytopenic purpura (TTP) by preventing the formation of microthrombi without severely compromising global hemostasis (Cablivi FDA Label). For adipose-derived platelets, ensuring the functionality of this interface is a key quality metric for their potential use as a cell therapy (Ono-Uruga et al., 2016).

Other names

vWF-GPIb interactionGPIb-vWF axisPlatelet glycoprotein Ib-alpha – von Willebrand factor complexvWF A1 domain – GPIbα interfacevon Willebrand factor – GPIbα interface on adipose-derived platelets

Inhibition of platelet adhesion to the subendothelial matrix by blocking the interaction between the A1 domain of von Willebrand factor and the N-terminal domain of platelet Glycoprotein Ib alpha (Cablivi FDA Label).