Cell Adhesion Inhibition by RGD Peptides Linked with a Photoisomerizable Nonnatural Amino Acid  

连接光异构化非天然氨基酸的RGD肽抑制细胞的附着(英文)

作　　者：张海黔[1,2] 篠原宽明 顾宁 佐々木裕司[2] 宍户昌彦 

机构地区：[1]吴健雄实验室,东南大学南京210096 [2]生物科学与技术系,冈山大学

出　　处：《Journal of Southeast University(English Edition)》2001年第2期22-26,共5页东南大学学报（英文版）

摘　　要：RGD peptides linked with a nonnatural amino acid, phenylazophenyl alaninine (azoAla), were synthesized and applied to cell adhesion inhibitors. The RGD peptides linked with azoAla at C terminal showed potent binding to the integrin on the surface of HeLa cells. Photoisomerization effect of the azobenzene side chain of synthesized peptides on the cell adhesion inhibition was further investigated. It was demonstrated that the cis form of azoAla linked RGD peptides revealed a little weak cell adhesion inhibition effect as compared with trans form of azoAla linked RGD peptide. 利用固相肽合成方法 ,将带有光敏基团偶氮苯的非天然氨基酸———苯基偶氮苯基苯丙氨酸与RGD肽连接 ,得到具有光敏功能的RGD肽 .非天然氨基酸连接在C端的RGD肽与HeLa细胞表面的整合素有很强的结合能力 .

关 键 词：nonnatural amino acid cell adhesion PHOTOISOMERIZATION INTEGRIN PEPTIDE 

分 类 号：Q517[生物学—生物化学] Q518.4