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作 者:刘莹[1] 范洪宽[1] 周慧[1] 王丽萍[1] 石玉华[1] 李惟[1]
机构地区:[1]吉林大学生命科学学院
出 处:《高等学校化学学报》1999年第5期744-746,共3页Chemical Journal of Chinese Universities
基 金:国家自然科学基金
摘 要:成纤维细胞生长因子(FGF)具有促进血管和神经形成的功能[1],但它在体内作用过度则经常伴随着肿瘤的发生[2].当前,研制和开发FGF拮抗剂,以有效地抑制FGF与细胞受体的结合,已成为国际性前沿课题.一种可行方法是设计合成FGF受体结合部位的亲和配体...Fibroblast growth factor(FGF) is known to bind to its cell surface receptor in a heparin dependent manner. By mimicking this in vivo process, we designed a novel screening strategy for the identification of FGF ligands that bind to the receptor binding region of FGF. After three cycles of selection, the phage recovery increased from 3.1×10 -4 % to 3.3×10 -3 %. The DNA inserts of phage clones were sequenced and a group of related peptide sequences were identified. Compared with a key FGF binding loop on the receptor (aa.342~357), these peptide sequences show similarities at several positions. Further ELISA experiment demonstrates that some phage containing these sequences can specifically bind to FGF. And cell proliferation assay suggest that the synthesized peptide can strongly inhibit the mitogenic activity of aFGF. Therefore, these peptides may specifically block the receptor binding to FGF and have the potential of becoming therapeutic agents as FGF antagonists.
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