Physical Isolation of Single Protein Molecules within Well‐Defined Coordination Cages to Enhance Their Stability

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.

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Publication Details

Journal
Angewandte Chemie International Edition
Published
2024-11-11
DOI
https://doi.org/10.1002/anie.202419476
Citations
12
Primary Topic
Chemical Synthesis and Analysis
Type
article
Field-Weighted Citation Impact
2.81

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article

Physical Isolation of Single Protein Molecules within Well‐Defined Coordination Cages to Enhance Their Stability

Sota Sato, Makoto Fujita, Masaaki Sugiyama, Risa Ebihara et al.
12 citations
Angewandte Chemie International Edition
Chemical Synthesis and Analysis
2.81
article

Physical Isolation of Single Protein Molecules within Well‐Defined Coordination Cages to Enhance Their Stability

Sota Sato, Makoto Fujita, Masaaki Sugiyama, Risa Ebihara, Maho Yagi‐Utsumi, Takahiro Nakama, Ken Morishima, Daishi Fujita
article en
12 citations

Abstract

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.

Angewandte Chemie International EditionVol. 64(7)
Mitsubishi Group (Japan) (JP), Osaka University of Health and Sport Sciences (JP), National Institutes of Natural Sciences (JP), Kyoto University (JP), Nagoya City University (JP), Institute for Molecular Science (JP), The Exploratory Research Center on Life and Living Systems (JP), The University of Tokyo (JP)
Japan Agency for Medical Research and Development, Japan Society for the Promotion of Science, Exploratory Research Center on Life and Living Systems, National Institutes of Natural Sciences
Openalex Percentile: Top 9%
Chemical Synthesis and Analysis
2.81
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