Expression and Purification of Optimized rolGLP-1, A Novel GLP-1 Analog, in Escherichia Coli BL21(DE3) and its Good Glucoregulatory Effect on Type 2 Diabetic Mice

ISSN: 1873-4316 (Online)
ISSN: 1389-2010 (Print)

Volume 18, 15 Issues, 2017

Download PDF Flyer

Current Pharmaceutical Biotechnology

This journal supports open access

Aims & ScopeAbstracted/Indexed in

Ranking and Category:
  • 152nd of 255 in Pharmacology & Pharmacy
  • 213th of 290 in Biochemistry & Molecular Biology

Submit Abstracts Online Submit Manuscripts Online

Zeno Foldes-Papp
Urban Clinical Center Soltau
University teaching hospital of Hamburg

View Full Editorial Board

Subscribe Purchase Articles Order Reprints

Current: 1.802
5 - Year: 2.327

Expression and Purification of Optimized rolGLP-1, A Novel GLP-1 Analog, in Escherichia Coli BL21(DE3) and its Good Glucoregulatory Effect on Type 2 Diabetic Mice

Current Pharmaceutical Biotechnology, 14(11): 985-994.

Author(s): Baicheng Ma, Peipei Tu, Xingyu Zhao, Yaofang Zhang, Yu Wang, Chao Ma, Yanli Ji, Xiaodan Li, Syed A. Abbas and Minggang Li.

Affiliation: Key Laboratory for Bioactive Materials of the Ministry of Education, Institute of Molecular Biology, College of Life Science, Nankai University, Tianjin 300071, P.R. China.


Glucagon-like peptide-1 (GLP-1) is an incretin hormone that decreases postprandial glycemic excursions by enhancing insulin secretion but with short half-life due to rapid inactivation by enzymatic N-terminal truncation. Therefore, efforts are being made to improve the stability of GLP-1 via modifying its structure or inhibiting dipeptidylpeptidase IV (DPP IV), which is responsible for its degradation. GLP-M, consisting of 10 tandem repeated rolGLP-1 (GLP-1 analog), has been expressed in Pichia pastoris by our laboratory. Although it had a long effect of maintaining glucose homeostasis, redundant amino acids and purification tag limited its application. Here, optimized rolGLP-1(GLPO) with no redundant amino acids and purification tag was constructed by molecular cloning and site-directed mutagenesis, which was expressed efficiently in Escherichia coli BL21(DE3) with the production of 81.5 mg/L, and confirmed by the results of SDS-PAGE electrophoresis and Western Blotting. Then GLP-O was purified via ion exchange chromatography and gel filtration chromatography. The purity of GLP-O was close to 100%. GLP-O could be cut into single rolGLP-1 by trypsin in vitro, and rolGLP-1 had anti-trypsin activity. After oral administration of GLP-O for 4 weeks, the level of blood glucose in type 2 diabetic mice was lowered effectively, and the oral glucose tolerance of mice was improved significantly. These results settled the foundation for further clinical application of GLP-O.


Diabetes, expression, GLP-1, Oral glucose tolerance, Purification, Western Blotting.

Purchase Online Order Reprints Order Eprints Rights and Permissions

Article Details

Volume: 14
Issue Number: 11
First Page: 985
Last Page: 994
Page Count: 10
DOI: 10.2174/1389201014666131226155553
Price: $58
Global Biotechnology Congress 2017Drug Discovery and Therapy World Congress 201711th Pharmaceutical Logistics event

Related Journals

Related eBooks

Webmaster Contact: Copyright © 2017 Bentham Science