Expression and Purification of Exendin-4 Dimer in Escherichia coli and Its Interaction with GLP-1 Receptor In Vitro

Author(s): Lina Yi , Xiaopu Yin , Dongzhi Wei , Yushu Ma .

Journal Name: Protein & Peptide Letters

Volume 13 , Issue 8 , 2006

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Abstract:

Exendin-4 is a 39 amino acid peptide isolated from the Gila monster salivary gland. It is 53% homologous to GLP-1 and exhibits similar glucoregulatory activities. In this study, exendin-4 dimer (D-Ex4) was constructed, cloned into plasmid pET32a(+) and expressed in E. coli BL21(DE3). The fusion protein with His-tag at the N-terminus was purified with a Ni-NTA-agarose column. After proteolytic cleavage, D-Ex4 peptide with high purity was obtained by HPLC. The results obtained by chemical cross-linking showed that D-Ex4 maintained affinity to GLP-1 receptor.

Keywords: Exendin-4 dimer, recombinant expression, purification, chemical cross-linking

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Article Details

VOLUME: 13
ISSUE: 8
Year: 2006
Page: [823 - 827]
Pages: 5
DOI: 10.2174/092986606777841226
Price: $58

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