Chemical Research in Chinese Universities ›› 2010, Vol. 26 ›› Issue (4): 604-607.

• Articles • Previous Articles     Next Articles

Screening and Identification of a Targeting Peptide to nGLP-1R from Phage Display Peptide Library

REN Hui1, XIONG Xin-hui2, JIANG Tao3, ZHANG Yang-de1*, WEI Zhong-hang3, SONG Xiang-wei2, GUAN Shu-wen2, WANG Yan3 and WANG Li-ping2,3*   

  1. 1. Center of Hepato-cholangio-intestinal Surgery of Ministry of Health, Xiangya Hospital, Central South University, Changsha 410008, P. R. China;
    2. College of Life Science, Jilin University, Changchun 130012, P. R. China;
    3. Department of General Surgery, China-Japan Union Hospital, Jilin University, Changchun 130033, P. R. China
  • Received:2010-03-15 Revised:2010-04-13 Online:2010-07-25 Published:2010-10-01
  • Contact: WANG Li-ping, E-mail: wanglp@jlu.edu.cn; ZHANG Yang-de, E-mail: zyd@2118.cn

Abstract: In order to provide the structure information for designing new exendin-4 analogues, a phage display peptide library was screened by targeting the N-terminal extracellular domain of GLP-1R(nGLP-1R). After four rounds of selection, nine sequences were obtained, four of them have higher affinity for nGLP-1R than the others. We chose two of them named X and Y peptides. Islet β-cell proliferation assay suggested that X and Y peptides didn’t have any activity to increase islet β-cell proliferation. In other words, X and Y peptides were not agonists to GLP-1R. However, the conservative motifs of X and Y peptides provided us useful information to design new exendin-4 analogues.

Key words: GLP-1 receptor, Phage display peptide library, Exendin-4