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

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

Volume: 13 Issue: 8

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

Affiliation:

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

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.

Cite this article as:

Yi Lina, Yin Xiaopu, Wei Dongzhi and Ma Yushu, Expression and Purification of Exendin-4 Dimer in Escherichia coli and Its Interaction with GLP-1 Receptor In Vitro, Protein & Peptide Letters 2006; 13(8) . https://dx.doi.org/10.2174/092986606777841226