Recent Development of Peptides from Glycoproteins IIb (αIIβ) and IIIa (β3) that Inhibit Platelet Fibrinogen Binding

Abstract

The glycoprotein (GP) IIb/IIIa (alphaIIbbeta3) found on platelets binds fibrinogen when platelets are activated, thereby mediating the platelet aggregation process. Blockading of alphaIIbbeta3 has been proposed to prevent platelet aggregation independent of the substance(s) responsible for activating the platelets. This inhibition of platelet aggregation is thought to be an effective therapeutic approach to various thromboembolic syndromes. The development of various forms of alphalambdapietaalpha;IIbbeta3 inhibitors has resulted in the inhibition of platelet aggregation, although studies of alphaIIbbeta3 receptor function and various alphaIIbbeta3 inhibitors have demonstrated the potential for these agents to produce effects on other aspects of platelet function as well as having non-platelet effects. This review describes the newly derived peptides from 1) glycoprotein IIb (alphaIIb) that interferes with platelet aggregation by inhibiting the binding of fibrinogen to alphaIIbbeta3 and from 2) GP IIIa (beta3) by blocking the alphaIIbbeta3 complex formation. These peptides may become effective agents to block the interaction of ADP, type I collagen, and type III collagen (type I collagen and type III collagen are present in abundant amounts in blood vessel walls) with platelets.