Expression of a glucagon-like peptide-1 analogue, as a therapeutic agent for type II diabetes, with enhanced bioactivity and increased N-terminal ... View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2015-11

AUTHORS

Kai Qian, Chengyuan Li, Xiaohai Gong, Charles Ndawula, Jin Qian, Yun Chen, Huazhong Li, Jian Jin

ABSTRACT

OBJECTIVE: To improve the bioactivity and increase the N-terminal homogeneity of a glucagon-like peptide-1 (GLP-1) analogue expressed in Pichia pastoris. RESULTS: The GLP-1 analogue. GGH, consisting of two tandem mutant GLP-1 (GLP-1[A2G]) fused with the N-terminus of human serum albumin (HSA), was expressed in P. pastoris. We also designed and expressed the novel GLP-1 analogue NGGH, which had a His-tag fused with the N-terminus of GGH and an enterokinase (EK) cleavage site at the fusion junction. The His-tag was removed by EK digestion to yield GGH2, which was subsequently compared with GGH expressed in P. pastoris. The purification recovery of GGH2 was 35 % compared with 23 % for GGH. Furthermore, the bioactivity of GGH2 was 605 % higher than GGH, and N-terminal homogeneity was also improved. CONCLUSIONS: A simple method for the preparation of GGH2 with a cleavable His-tag was developed, and the resultant protein possessed improved bioactivity and N-terminal homogeneity. More... »

PAGES

2229-2235

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s10529-015-1900-7

DOI

http://dx.doi.org/10.1007/s10529-015-1900-7

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1052332582

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/26160109


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