Production of a therapeutic protein by fusing it with two fragments of the carboxyl-terminal peptide of human chorionic gonadotropin β-subunit in Pichia pastoris

Objective To produce a therapeutic protein (endostatin) by fusion with two fragments of the carboxyl-terminal peptide (CTP) of the human chorionic gonadotropin β-subunit in Pichia pastoris . Results Two CTP sequences were fused to the C -terminal of human endostatin, and the fusion protein (endo-CTP) was expressed by P. pastoris . Endo-CTP inhibited proliferation of endothelial cells with an IC 50 of 7 μg ml −1 , and 30 % of cells were annexin V-positive after treatment with 20 μg endo-CTP ml −1 for 48 h. Migration of endothelial cells was inhibited by endo-CTP in a concentration-dependent manner. The half-life of endo-CTP in Sprague–Dawley rats was much longer than that of its commercial counterpart (Endostar). Conclusion A long-acting endostatin can be produced using CTP technology.