Protein stabilization and refolding in a gigantic self-assembled cage
Protein stabilization and refolding in a gigantic self-assembled cage
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DOI：
10.1016/j.chempr.2021.08.005
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发表时间：
2021-10-14
期刊：
影响因子：
23.5
通讯作者：
Fujita, Makoto
中科院分区：
文献类型：
--
作者：
Fujita, Daishi;Suzuki, Ryoto;Fujita, Makoto
分子的空间隔离通常是调节其分子行为的有力策略。生物系统很好地利用了这种机制;然而，科学家们还没有与自然相匹敌，特别是在大分子底物方面。我们证明了将蛋白质封装在具有开放框架的分子笼中可以稳定蛋白质的三级结构并提高其酶活性。特别地，当三维限制的酶暴露于有机溶剂时，其半衰期延长1,000倍。酶促反应的动力学和光谱分析表明，这种稳定性的关键是孤立的空间;这让人想起伴侣蛋白，它使用它们的大内腔来帮助客户蛋白的折叠。单分子蛋白质笼提供了一种新型的基于蛋白质的纳米生物技术，加速了分子生物学研究和工业应用。
Spatial isolation of molecules is often a powerful strategy for regulating their molecular behavior. Biological systems employ such mechanisms well; however, scientists have yet to rival nature, particularly for macromolecular substrates. We demonstrated that the encapsulation of a protein in a molecular cage with an open framework stabilizes the tertiary structure of the protein and improves its enzymatic activity. Particularly, when the three-dimensionally confined enzyme was exposed to an organic solvent, its half-life was prolonged 1,000-fold. Kinetic and spectroscopic analysis of the enzymatic reaction revealed that the key to this stability is the isolated space; this is reminiscent of chaperonins, which use their large internal cavities to assist the folding of client proteins. The single-molecule protein caging affords a new type of protein-based nanobiotechnology that accelerates molecular biology research as well as industrial applications.