Dynamic protein self-assembly driven by host–guest chemistry and the folding–unfolding feature of a mutually exclusive protein

Ruidi Wang; Shanpeng Qiao; Linlu Zhao; Chunxi Hou; Xiumei Li; Yao Liu; Quan Luo; Jiayun Xu; Hongbin Li; Junqiu Liu

doi:10.1039/C7CC05745H

Dynamic protein self-assembly driven by host–guest chemistry and the folding–unfolding feature of a mutually exclusive protein†

Ruidi Wang,^a Shanpeng Qiao,^a Linlu Zhao,^a Chunxi Hou,^a Xiumei Li,^a Yao Liu,^a Quan Luo,^a Jiayun Xu,^a Hongbin Li*^b and Junqiu Liu

*^a

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^a State Key Laboratory of Supramolecular Structure and Materials, College of Chemistry, Jilin University, 2699 Qianjin Street, Changchun 130012, People's Republic of China
E-mail: junqiuliu@jlu.edu.cn

^b Department of Chemistry, The University of British Columbia, Vancouver, BC V6T 1Z1, Canada
E-mail: Hongbin@chem.ubc.ca

Abstract

A novel exploration utilizing a well-designed fusion protein containing a redox stimuli-responsive domain was developed to construct dynamic protein self-assemblies induced by cucurbit[8]uril-based supramolecular interactions. The reversible interconversion of the morphology of the assemblies between nanowires and nanorings was regulated precisely by redox conditions.

Chemical Communications

Dynamic protein self-assembly driven by host–guest chemistry and the folding–unfolding feature of a mutually exclusive protein†

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Dynamic protein self-assembly driven by host–guest chemistry and the folding–unfolding feature of a mutually exclusive protein

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