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

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.