Matsumura Sachiko, Uemura Shinobu, Mihara Hisakazu
Corporate Research Laboratory, Corporate Research Group, Fuji Xerox Co. Ltd., 430 Sakai, Nakai-machi, Ashigarakami-gun, Kanagawa 259-0157, Japan.
Mol Biosyst. 2005 Jul;1(2):146-8. doi: 10.1039/b504516a. Epub 2005 Jun 24.
Three kinds of biotinylated peptides with different linkers between biotin and beta-sheet peptide were designed and synthesized. The transmission electron microscopy revealed that the biotinylated peptides self-assembled to form a tubular structure with external diameter of ca. 60 nm and inner diameter of ca. 30 nm in an aqueous solution. The anti-biotin antibody effectively bound to biotin groups in the peptide nanotubes. The binding of antibody was regulated by not only the concentration of the protein in the solution but also the properties of biotinylated peptides forming the tubes. The antibody preferentially bound to the biotinylated peptide tubes assembled from the peptide with the most hydrophilic linker, suggesting that the surface properties and functions of the tubular structure were modulated and engineered by the design of the peptides.
设计并合成了三种在生物素与β-折叠肽之间具有不同连接子的生物素化肽。透射电子显微镜显示，生物素化肽在水溶液中自组装形成外径约60 nm、内径约30 nm的管状结构。抗生物素抗体能有效结合肽纳米管中的生物素基团。抗体的结合不仅受溶液中蛋白质浓度的调节，还受形成纳米管的生物素化肽的性质调节。抗体优先结合由具有最亲水连接子的肽组装而成的生物素化肽管，这表明通过肽的设计可以调节和改造管状结构的表面性质和功能。
