高等学校化学研究 ›› 2010, Vol. 26 ›› Issue (4): 604-607.
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*
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*
摘要: 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.