由主客体化学和互斥蛋白的折叠-去折叠特性驱动的动态蛋白质自组装。
Dynamic protein self-assembly driven by host-guest chemistry and the folding-unfolding feature of a mutually exclusive protein.
作者信息
Wang Ruidi, Qiao Shanpeng, Zhao Linlu, Hou Chunxi, Li Xiumei, Liu Yao, Luo Quan, Xu Jiayun, Li Hongbin, Liu Junqiu
机构信息
State Key Laboratory of Supramolecular Structure and Materials, College of Chemistry, Jilin University, 2699 Qianjin Street, Changchun 130012, People's Republic of China.
出版信息
Chem Commun (Camb). 2017 Sep 21;53(76):10532-10535. doi: 10.1039/c7cc05745h.
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.
利用一种精心设计的含有氧化还原刺激响应域的融合蛋白进行了一项新颖的探索，以构建由基于葫芦[8]脲的超分子相互作用诱导的动态蛋白质自组装体。组装体在纳米线和纳米环之间的形态可逆相互转化通过氧化还原条件精确调控。
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