Expression and characterization of Momordica Chanrantia anti-hyperglycaemic peptide in Escherichia coli |
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| Authors: | Si-Xiu Liu Zhong-Ping Fu Rui-Min Mu Zhi-Bi Hu Fu-Jun Wang Xiang-Rong Wang |
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| Affiliation: | (1) Department of Environmental Science & Engineering, Urban Eco-Planning & Design Researching Center, Fudan University, 200433 Shanghai, People’s Republic of China;(2) Institute of Traditional Chinese Medicine, Shanghai University of Traditional Chinese Medicine, 201203 Shanghai, China |
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| Abstract: | A nucleic acid sequence MC, encoding Momordica Chanrantia anti-hyperglycaemic peptide MC6 (accession: AAX06814) synthesized according to Escherichia coli preferred codons, was cloned and expressed in E. coli. Recombinant protein pQE8-MC (about 3.5 kDa) was purified and analyzed by 20% SDS–PAGE and western blot. It revealed that the expressed pQE8-MC had good solubility in aqueous media. An HPLC assay was used to confirm the expression of pQE8-MC. Subsequent pharmacological activity assay revealed a significant hypoglycemic effect of low dose treatments of pQE8-MC on male kunming mice. Four hours after an intravenous tail injection, the blood sugar levels of mice treated with pQE8-MC saline solution A3 (1 mg/kg BW) decreased greatly (P < 0.01) relative to the levels of a control group. This suggests that pQE8-MC, expressed in bioengineered E. coli, has a similar hypoglycemic function to the natural protein MC6 from M. Chanrantia. These results reveal the possibility of using bio-engineered bacteria as an anti-diabetic agent. |
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