Tetrafibricin is a novel nonpeptidic fibrinogen receptor isolated from the culture broth of Streptomyces neyagawaensis NR0577. Tetrafibricin competitively inhibited (Ki = 9.9 nM) the binding of biotinylated fibrinogen to purified active glycoprotein GPIIb/IIIa immobilized on plastic plate. Tetrafibricin strongly inhibited the binding of fibrinogen to its receptors with an IC50 of 46 nM. It also inhibited ADP-, collagen-, and thrombin-induced aggregation of human platelets with IC50s of 5.6, 11.0 and 7.6 µM, respectively. To our knowledge, there is no total synthesis of tetrafibricin done yet. Only two papers have been published toward the total synthesis of tetrafibricin. Cossy’s group synthesized the C1-C13, C15-C25, C27-C40 fragments of tetrafibricin by a sequence of chemoselective cross-metathesis reactions and enantioselective allyltitanations of aldehydes. And Roush’s group reported the synthesis of the C1-C19 fragment of tetrafibricin via a highly diastereoselective double allylboration developed in their laboratory.