Abolishes platelet aggregation induced by collagen, ADP (IC(50)=292 nM) and arachidonic-acid. The inhibition of collagen-induced platelet aggregation may be due to its ability to bind collagen and block the binding site on collagen for platelets and/or to its ability to bind to the platelet alpha-2/beta-1 collagen receptor (ITGA2/ITGB1) to block its interaction with collagen and hence prevent platelet stimulation. The inhibition of ADP- or arachidonic-acid-induced platelet aggregation may be due to it acting as an antagonist of the ADP receptors or thromboxane-prostanoid receptors of the platelets, respectively. Does not interact with integrins alpha-IIb (ITGA2B) or beta-3 (ITGB3) nor platelet glycoproteins VI (GP6) or IX (GP9) in vitro, however, the detection is dependent on experimental conditions and may happen in vivo. Able to bind to platelet glycoprotein Ib alpha chain (GP1BA) receptor in vitro, although this interaction may have pathologically only limited effect in vivo as it is not able to abolish the von Willebrand factor (vWF)-dependent platelet agglutination induced by ristocetin. Does not affect blood coagulation