title: Nanoscale elongating control of the self-assembled protein filament with the cysteine-introduced building blocks.
abstract: Self-assembly of artificially designed proteins is extremely desirable for nanomaterials. Here we show a novel strategy for the creation of self-assembling proteins, named "Nanolego." Nanolego consists of "structural elements" of a structurally stable symmetrical homo-oligomeric protein and "binding elements," which are multiple heterointeraction proteins with relatively weak affinity. We have established two key technologies for Nanolego, a stabilization method and a method for terminating the self-assembly process. The stabilization method is mediated by disulfide bonds between Cysteine-residues incorporated into the binding elements, and the termination method uses "capping Nanolegos," in which some of the binding elements in the Nanolego are absent for the self-assembled ends. With these technologies, we successfully constructed timing-controlled and size-regulated filament-shape complexes via Nanolego self-assembly. The Nanolego concept and these technologies should pave the way for regulated nanoarchitecture using designed proteins.
authors.affiliation: CREST, Japan Science and Technology Agency, Kawaguchi, Saitama 332-0012, Japan.
authors.forename: Kengo
authors.initials: K
authors.lastname: Usui
authors.forename: Tei
authors.initials: T
authors.lastname: Maki
authors.forename: Fuyu
authors.initials: F
authors.lastname: Ito
authors.forename: Atsushi
authors.initials: A
authors.lastname: Suenaga
authors.forename: Satoru
authors.initials: S
authors.lastname: Kidoaki
authors.forename: Masayoshi
authors.initials: M
authors.lastname: Itoh
authors.forename: Makoto
authors.initials: M
authors.lastname: Taiji
authors.forename: Takehisa
authors.initials: T
authors.lastname: Matsuda
authors.forename: Yoshihide
authors.initials: Y
authors.lastname: Hayashizaki
authors.forename: Harukazu
authors.initials: H
authors.lastname: Suzuki
mesh_terms: D000818:Animals; D003198:Computer Simulation; D004220:Disulfides / Q000378:metabolism; D006801:Humans; D051379:Mice; D008958:Models, Molecular; D049329:Nanostructures / Q000737:chemistry / Q000648:ultrastructure; D036103:Nanotechnology / Q000379:methods*; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D011485:Protein Binding; D015202:Protein Engineering; D055503:Protein Multimerization; D055550:Protein Stability; D011506:Proteins / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure
chemical_list: D004220:Disulfides; D010446:Peptide Fragments; D011506:Proteins; D011994:Recombinant Proteins