科研之友
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摘要
Glucagon-like peptide-1 (GLP-1) is a natural incretin hormone released from intestinal L-cells in response to hormonal, neural and nutrient stimuli. Liraglutide is derived from human GLP-1 by substituting Lys34 with Arg and conjugating a palmitic acid to Lys26 via a glutamate spacer, which has a long-lasting hypoglycemic effect. The precursor of liraglutide is a K34R mutant of GLP-1 (GLP-1(R34)) and was produced previously by either yeast protein expression system or peptide solid phase synthesis. However, degradation of secreted proteins limits the effectiveness of yeast protein expression system and peptide solid phase synthesis requires the use of large amounts of organic solvents and expensive condensation agents. In this study, we reported a novel method to prepare GLP-1(R34) using E. coil protein expression system. The GLP-1(R34) peptide was overexpressed as an MFH-GLP-1(R34) fusion protein and was released from the fusion protein through formic acid cleavage. The target peptide was purified by reverse-phase chromatography and ion exchange chromatography. Our work demon. strated a high-productive process for large-scale preparation of the liraglutide precursor with high purity.
- 出版日期2017-11
- 单位湖北工业大学
