Construction of biotinylated peptide nanotubes for arranging proteins.
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.
Matsumura
Sachiko
S
Corporate Research Laboratory, Corporate Research Group, Fuji Xerox Co. Ltd., 430 Sakai, Nakai-machi, Ashigarakami-gun, Kanagawa 259-0157, Japan.
Uemura
Shinobu
S
Mihara
Hisakazu
H
D000595:Amino Acid Sequence; D000906:Antibodies / Q000378:metabolism; D019921:Biotinylation / Q000379:methods; D046529:Microscopy, Electron, Transmission / Q000379:methods; D008958:Models, Molecular; D045333:Nanotubes, Peptide / Q000737:chemistry* / Q000648:ultrastructure; D011485:Protein Binding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D017550:Spectroscopy, Fourier Transform Infrared / Q000379:methods
D000906:Antibodies; D045333:Nanotubes, Peptide; D011506:Proteins