Literature DB >> 19585270

Expression and characterization of Momordica Chanrantia anti-hyperglycaemic peptide in Escherichia coli.

Si-Xiu Liu1, Zhong-Ping Fu, Rui-Min Mu, Zhi-Bi Hu, Fu-Jun Wang, Xiang-Rong Wang.   

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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Year:  2009        PMID： 19585270     DOI： 10.1007/s11033-009-9609-0

Source DB:  PubMed          Journal:  Mol Biol Rep        ISSN： 0301-4851            Impact factor:   2.316


  22 in total

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