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

Lina Yi; Xiaopu Yin; Dongzhi Wei; Yushu Ma

doi:10.2174/092986606777841226

ISSN: 0929-8665
E-ISSN: 1875-5305

Expression and Purification of Exendin-4 Dimer in Escherichia coli and Its Interaction with GLP-1 Receptor In Vitro
Authors: Lina Yi¹, Xiaopu Yin², Dongzhi Wei³ and Yushu Ma⁴
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¹ State Key Laboratory of Bioreactor Engineering, Institute of Biochemistry, East China University of Science and Technology, Shanghai, 200237, China. ² State Key Laboratory of Bioreactor Engineering, Institute of Biochemistry, East China University of Science and Technology, Shanghai, 200237, China. ³ State Key Laboratory of Bioreactor Engineering, Institute of Biochemistry, East China University of Science and Technology, Shanghai, 200237, China. ⁴ State Key Laboratory of Bioreactor Engineering, Institute of Biochemistry, East China University of Science and Technology, Shanghai, 200237, China.
Source: Protein and Peptide Letters, Volume 13, Issue 8, Aug 2006, p. 823 - 827
DOI: https://doi.org/10.2174/092986606777841226
- Available online: 01 Aug 2006

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.

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2006-08-01

2025-05-29

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Article Type: Research Article

Keyword(s): chemical cross-linking; Exendin-4 dimer; purification; recombinant expression

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

Abstract

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