Hirano Y, Okuno M, Hayashi T, Goto K, Nakajima A
Department of Applied Chemistry, Osaka Institute of Technology, Japan.
J Biomater Sci Polym Ed. 1993;4(3):235-43. doi: 10.1163/156856293x00546.
Tetrapeptides, Arg-Gly-Asp-Ser (RGDS), Arg-Gly-Asp-Val (RGDV), and Arg-Gly-Asp-Thr (RGDT), respectively, appearing in the cell-attachment domains of fibronectin, vitronectin, and collagen, and pentapeptide Tyr-Ile-Gly-Ser-Arg (YIGSR) appearing in B1 chain of laminin, were synthesized by liquid-phase procedure. Bioactivities of RGD, RGDX (X = S, V and T), YIGSR, and YIGSR-NH2 as cell recognition determinants were investigated by cell-attachment test using these oligopeptides immobilized to ethylene-acrylic acid copolymer (PEA) film. The cell lines used were A431, NRK, CHO-K1, HeLa.S3, and RLC-16 cells. It was found that the residue X in RGDX plays an important role for cell-attachment activity of RGDX, and, regarding YIGSR, introduction of NH2 residue at the C-terminal of the pentapeptide enhances the cell-attachment activity.
分别出现在纤连蛋白、玻连蛋白和胶原蛋白细胞附着结构域中的四肽Arg-Gly-Asp-Ser（RGDS）、Arg-Gly-Asp-Val（RGDV）和Arg-Gly-Asp-Thr（RGDT），以及出现在层粘连蛋白B1链中的五肽Tyr-Ile-Gly-Ser-Arg（YIGSR），通过液相法合成。使用固定在乙烯-丙烯酸共聚物（PEA）膜上的这些寡肽，通过细胞附着试验研究了RGD、RGDX（X = S、V和T）、YIGSR以及YIGSR-NH2作为细胞识别决定簇的生物活性。所使用的细胞系为A431、NRK、CHO-K1、HeLa.S3和RLC-16细胞。发现RGDX中的残基X对RGDX的细胞附着活性起重要作用，并且就YIGSR而言，在五肽的C末端引入NH2残基可增强细胞附着活性。
