期刊
NATURE COMMUNICATIONS
卷 7, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms10619
关键词
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资金
- Army Research Office [W911NF-11-1-0137]
- Army Research Office MURI award [W911NF-12-1-0420]
- National Science Foundation [1033222]
- NIH Transformative award [R01GM104960]
- National Science Foundation of China [21329501]
- Presidential Strategic Initiative Fund from Arizona State University
- Army Research Office YIP award [W911NF-14-1-0434]
- Rutgers University
- Div Of Chem, Bioeng, Env, & Transp Sys
- Directorate For Engineering [1033222] Funding Source: National Science Foundation
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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