[Cloning expression and characterization of a multifunctional anticoagulated peptide gene in E. Coli].

Objective: To investigate the feasibility about the cloning, expression and characterization of multifunctional anticoagulated peptide.

Methods: We designed a construct using glutathione S-transferase (GST) as a protein vector, fused via a cleavable linker to an antithrombotic peptide of 31 amino acids. The peptide was designed to include three inhibitory regions: (1) the Lys-Gly-Asp (KGD) amino acid sequence to prevent fibrinogen binding to platelets; (2) a part of fibrinopeptide A, an inhibitor of thrombin; and (3) the tail of hirudin, a potent direct antithrombin.