title: Protein assemblies by site-specific avidin-biotin interactions.
abstract: Exploiting self-assembly systems with biological building blocks is of significant interest in the fabrication of advanced biomaterials. We assessed the potential use of site-specific ligand labeling of protein building blocks in designing functional protein self-assemblies by combining site-specifically biotinylated bacterial alkaline phosphatase (as a bidentate or tetradentate ligand unit) and streptavidin (as a tetrameric receptor).
authors: Department of Applied Chemistry, Graduate School of Engineering, Kyushu University, Fukuoka, Japan.
authors: Yutaro
authors: Y
authors: Mori
authors: Kosuke
authors: K
authors: Minamihata
authors: Hiroki
authors: H
authors: Abe
authors: Masahiro
authors: M
authors: Goto
authors: Noriho
authors: N
authors: Kamiya
mesh_terms: D000469:Alkaline Phosphatase / Q000378:metabolism; D000595:Amino Acid Sequence; D001360:Avidin / Q000378:metabolism*; D001419:Bacteria / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism*; D001710:Biotin / Q000378:metabolism*; D008024:Ligands; D008969:Molecular Sequence Data; D019809:Streptavidin / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D008024:Ligands; D001360:Avidin; D001710:Biotin; D019809:Streptavidin; D000469:Alkaline Phosphatase