Ebihara Risa, Nakama Takahiro, Morishima Ken, Yagi-Utsumi Maho, Sugiyama Masaaki, Fujita Daishi, Sato Sota, Fujita Makoto
Department of Applied Chemistry, School of Engineering, The University of Tokyo, Mitsui Link Lab Kashiwanoha 1, FS CREATION, 6-6-2 Kashiwanoha, Kashiwa, Chiba, 277-0882, Japan.
Institute for Integrated Radiation and Nuclear Science, Kyoto University, Kumatori, Sennan-gun, Osaka, 590-0494, Japan.
Angew Chem Int Ed Engl. 2025 Feb 10;64(7):e202419476. doi: 10.1002/anie.202419476. Epub 2024 Nov 20.
Encapsulation of a single protein within a confined space can lead to distinct properties compared to bulk solutions, but controlling the number of encapsulated proteins and their environment remains challenging. This study demonstrates the encapsulation of single proteins within well-defined, tunable cavities of self-assembled coordination cages, thereby enhancing protein stability. Within uniform cavities of size-tunable coordination cages, 15 different proteins of varying sizes (3-6 nm in diameter) and properties (e.g., isoelectric points and hydrophobicity) were successfully confined. Various analytical techniques confirmed that the proteins maintained their secondary structures and enzymatic activities under denaturing conditions such as exposure to organic solvents, heat, and buffers. These findings suggest that such coordination cages have the potential to serve as synthetic hosts for precisely controlling protein functions within their customizable cavities.
与本体溶液相比，将单个蛋白质封装在受限空间中可导致不同的性质，但控制封装蛋白质的数量及其环境仍然具有挑战性。本研究展示了将单个蛋白质封装在自组装配位笼的明确、可调谐的腔内，从而提高了蛋白质的稳定性。在尺寸可调谐配位笼的均匀腔内，成功封装了15种不同大小（直径3-6 nm）和性质（如等电点和疏水性）的蛋白质。各种分析技术证实，这些蛋白质在诸如暴露于有机溶剂、加热和缓冲液等变性条件下仍保持其二级结构和酶活性。这些发现表明，这种配位笼有潜力作为合成宿主，在其可定制的腔内精确控制蛋白质功能。
