Dynamic protein self-assembly driven by host–guest chemistry and the folding–unfolding feature of a mutually exclusive protein. Issue 76 (11th September 2017)

• Record Type: Journal Article
• Authors: Wang, Ruidi; Qiao, Shanpeng; Zhao, Linlu; Hou, Chunxi; Li, Xiumei; Liu, Yao; Luo, Quan; Xu, Jiayun; Li, Hongbin; Liu, Junqiu
• Is Part Of: Chemical communications. Volume 53:Issue 76(2017)
• Page Start: 10532
• Page End: 10535
• Publication Date: 2017-09-11
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/c7cc05745h
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : Taking advantage of cucurbit[8]uril-based supramolecular interactions, we constructed a novel redox-responsive assembly which was controllable to transform the morphology. 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.