The ChemDiv library contains 27 000 compounds targeted at Macl-GPIb alpha Interaction.
Leukocyte-platelet interaction is important in mediating leukocyte adhesion to a thrombus and leukocyte recruitment to a site of vascular injury. This interaction is mediated by the β2-integrin Mac-1 (also known as integrin αMβ2) and its counter-receptor on platelets, glycoprotein Ibalpha (GPIb), a component of the GP Ib-IX-V complex, the platelet von Willebrand factor (vWf) receptor. 
Studies showed that the Macl-GPIb alpha interaction involves the Mac-1 I domain (homologous to the vWf A1 domain), and the GPIb leucine-rich repeat and COOH-terminal flanking regions. Since leukocyte–platelet interactions bidirectionally induce signals that amplify pro-inflammatory and pro-thrombotic cellular responses, it provides a molecular target for disrupting leukocyte-platelet complexes that promote vascular inflammation in thrombosis, atherosclerosis, and angioplasty-related restenosis. 
Current antithrombotic drugs, including antiplatelet agents and anticoagulants, are associated with significant bleeding risk and increased mortality. It was shown that small-molecule targeting of Mac-1-GPIb interaction successfully inhibits thrombosis. Moreover, it was identified that targeting this interaction has antithrombotic therapeutic potential with reduced bleeding risk. 
 Y. Wang et al., “Leukocyte integrin Mac-1 regulates thrombosis via interaction with platelet GPIbα,” Nat. Commun., vol. 8, no. May, 2017, doi: 10.1038/ncomms15559.
 D. I. Simon et al., “Platelet glycoprotein Ibα is a counterreceptor for the leukocyte integrin Mac-1 (CD11b/CD18),” J. Exp. Med., vol. 192, no. 2, pp. 193–204, 2000, doi: 10.1084/jem.192.2.193.