Ligand-receptor interaction-induced self-assembled architectures of proteins: Characterization of the interaction forces and manner of assembly NanoLEGO proteins

Tei Maki, Kengo Usui, Satoru Kidoaki, Harukazu Suzuki, Masayoshi Ito, Fuyu Ito, Takehisa Matsuda, Yoshihide Hayashizaki

Research output: Contribution to conferencePaperpeer-review

Abstract

We have constructed the fusion proteins which contain multiple different specific binding sites and self-assemble to an ordered structure by their mutual specific interactions (termed NanoLEGO). Subunit of tetramer protein, super oxide reductase (SOR), was fused with PDZ protein, tax-interacting protein-1(TIP-1), and its recognition peptides(PDZ-pep). The genetically-modified subunits of SOR with TIP-1 and PDZ-pep could self-assemble and reconstruct the chimera tetramer with four binding sites. To investigate the self-assembling ability of SOR NanoLEGO, the interaction forces between TIP-1 and PDZ-pep were characterized by dynamic force spectroscopy, and the assembling property and structures were analyzed with turbidity measurement, phase contrast and fluorescence microscopy, and transmission electron microscopy. SOR NanoLEGOs were found to self-assemble and form chain-like constructs.

Original languageEnglish
Pages5284-5285
Number of pages2
Publication statusPublished - Dec 1 2006
Event55th Society of Polymer Science Japan Symposium on Macromolecules - Toyama, Japan
Duration: Sep 20 2006Sep 22 2006

Other

Other55th Society of Polymer Science Japan Symposium on Macromolecules
CountryJapan
CityToyama
Period9/20/069/22/06

All Science Journal Classification (ASJC) codes

  • Engineering(all)

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