Abstract
A phage display library of exendin-4 mutants was screened with the extracellular domain of rat glucagon-like peptide 1 receptor as the target. A novel variant of exendin-4 with higher affinity for the receptor fraction than that of the wild type was identified. The increased affinity was attributed to the substitution of Glu16 by Val16. Although the substitution probably caused an increased entropic cost to the helix region, the linker around Val16 is more flexible resulting in the increase of affinity for the receptor.
Keywords: Exendin-4, GLP-1 receptor, phage display library
Protein & Peptide Letters
Title: Screening of a Phage Display Library of Exendin-4 Mutants with the Extracellular Domain of Rat GLP-1 Receptor
Volume: 14 Issue: 8
Author(s): Xiaopu. Yin, Yushu Ma, Meiyun Liu, Weifeng Gao and Dongzhi Wei
Affiliation:
Keywords: Exendin-4, GLP-1 receptor, phage display library
Abstract: A phage display library of exendin-4 mutants was screened with the extracellular domain of rat glucagon-like peptide 1 receptor as the target. A novel variant of exendin-4 with higher affinity for the receptor fraction than that of the wild type was identified. The increased affinity was attributed to the substitution of Glu16 by Val16. Although the substitution probably caused an increased entropic cost to the helix region, the linker around Val16 is more flexible resulting in the increase of affinity for the receptor.
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Cite this article as:
Xiaopu. Yin , Yushu Ma , Meiyun Liu , Weifeng Gao and Dongzhi Wei , Screening of a Phage Display Library of Exendin-4 Mutants with the Extracellular Domain of Rat GLP-1 Receptor, Protein & Peptide Letters 2007; 14 (8) . https://dx.doi.org/10.2174/092986607781483679
DOI https://dx.doi.org/10.2174/092986607781483679 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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