Issue 4, 2019

Construction of supramolecular nanotubes from protein crystals


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

Supplementary files

Article information

Article type
Edge Article
19 Sep 2018
26 Oct 2018
First published
30 Oct 2018
This article is Open Access

All publication charges for this article have been paid for by the Royal Society of Chemistry
Creative Commons BY license

Chem. Sci., 2019,10, 1046-1051

Construction of supramolecular nanotubes from protein crystals

T. K. Nguyen, H. Negishi, S. Abe and T. Ueno, Chem. Sci., 2019, 10, 1046 DOI: 10.1039/C8SC04167A

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