Premium
Nanoscale elongating control of the self‐assembled protein filament with the cysteine‐introduced building blocks
Author(s) -
Usui Kengo,
Maki Tei,
Ito Fuyu,
Suenaga Atsushi,
Kidoaki Satoru,
Itoh Masayoshi,
Taiji Makoto,
Matsuda Takehisa,
Hayashizaki Yoshihide,
Suzuki Harukazu
Publication year - 2009
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.106
Subject(s) - protein filament , cysteine , self assembly , nanotechnology , nanomaterials , disulfide bond , nanoscopic scale , chemistry , biophysics , materials science , biochemistry , biology , enzyme
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.