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Construction of supramolecular nanotubes from protein crystals

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Abstract

Investigations involving the design of protein assemblies for the development of biomaterials are receiving significant attention. In nature, proteins can be driven into assemblies frequently by various non-covalent interactions. Assembly of proteins into supramolecules can be conducted under limited conditions in solution. These factors force the assembly process into an equilibrium state with low stability. Here, we report a new method for preparing assemblies using protein crystals as non-equilibrium molecular scaffolds. Protein crystals provide an ideal environment with a highly ordered packing of subunits in which the supramolecular assembled structures are formed in the crystalline matrix. Based on this feature, we demonstrate the self-assembly of supramolecular nanotubes constructed from protein crystals triggered by co-oxidation with cross-linkers. The assembly of tubes is driven by the formation of disulfide bonds to retain the intermolecular interactions within each assembly in the crystalline matrix after dissolution of the crystals.

Graphical abstract: Construction of supramolecular nanotubes from protein crystals

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Publication details

The article was received on 19 Sep 2018, accepted on 26 Oct 2018 and first published on 30 Oct 2018


Article type: Edge Article
DOI: 10.1039/C8SC04167A
Citation: Chem. Sci., 2019, Advance Article
  • Open access: Creative Commons BY license
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    Construction of supramolecular nanotubes from protein crystals

    T. K. Nguyen, H. Negishi, S. Abe and T. Ueno, Chem. Sci., 2019, Advance Article , DOI: 10.1039/C8SC04167A

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