Cells routinely compartmentalize enzymes for enhanced efficiency of their metabolic pathways. Here we report a general approach to construct DNA nanocaged enzymes for enhancing catalytic activity and stability. Nanocaged enzymes are realized by self-assembly into DNA nanocages with well-controlled stoichiometry and architecture that enabled a systematic study of the impact of both encapsulation and proximal polyanionic surfaces on a set of common metabolic enzymes. Activity assays at both bulk and single-molecule levels demonstrate increased substrate turnover numbers for DNA nanocage-encapsulated enzymes. Unexpectedly, we observe a significant inverse correlation between the size of a protein and its activity enhancement. This effect is consistent with a model wherein distal polyanionic surfaces of the nanocage enhance the stability of active enzyme conformations through the action of a strongly bound hydration layer. We further show that DNA nanocages protect encapsulated enzymes against proteases, demonstrating their practical utility in functional biomaterials and biotechnology.
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- Nanocaged Enzymes With Enhanced Catalytic Activity and Increased Stability Against Protease Digestion
- Zhao, Zhao (Author)
- Fu, Jinglin (Author)
- Dhakal, Soma (Author)
- Johnson-Buck, Alexander (Author)
- Liu, Minghui (Author)
- Zhang, Ting (Author)
- Woodbury, Neal (Author)
- Liu, Yan (Author)
- Walter, Nils G. (Author)
- Yan, Hao (Author)
- Biodesign Institute (Contributor)
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Digital object identifier: 10.1038/ncomms10619
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Identifier TypeInternational standard serial numberIdentifier Value2041-1723
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The final version of this article, as published in Nature Communications, can be viewed online at: http://www.nature.com/articles/ncomms10619
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Zhao, Z., Fu, J., Dhakal, S., Johnson-Buck, A., Liu, M., Zhang, T., . . . Yan, H. (2016). Nanocaged enzymes with enhanced catalytic activity and increased stability against protease digestion. Nature Communications, 7, 10619. doi:10.1038/ncomms10619