Unknown

Dataset Information

0

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.

SUBMITTER: Usui K 

PROVIDER: S-EPMC2771298 | biostudies-literature | 2009 May

REPOSITORIES: biostudies-literature

altmetric image

Publications

Nanoscale elongating control of the self-assembled protein filament with the cysteine-introduced building blocks.

Usui Kengo K   Maki Tei T   Ito Fuyu F   Suenaga Atsushi A   Kidoaki Satoru S   Itoh Masayoshi M   Taiji Makoto M   Matsuda Takehisa T   Hayashizaki Yoshihide Y   Suzuki Harukazu H  

Protein science : a publication of the Protein Society 20090501 5


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  ...[more]

Similar Datasets

| S-EPMC10142354 | biostudies-literature
2024-09-03 | GSE242885 | GEO
| S-EPMC6647868 | biostudies-literature
| S-EPMC8695017 | biostudies-literature
| S-EPMC9784872 | biostudies-literature
| S-EPMC4521158 | biostudies-literature
| S-EPMC8400969 | biostudies-literature
| S-EPMC4973615 | biostudies-literature
| S-EPMC5412948 | biostudies-literature
| S-EPMC7311176 | biostudies-literature