Nanocaged enzymes with enhanced catalytic activity and increased stability against protease digestion

Zhao Zhao, Jinglin Fu (), Soma Dhakal, Alexander Johnson-Buck, Minghui Liu, Ting Zhang, Neal W. Woodbury, Yan Liu, Nils G. Walter () and Hao Yan ()
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Zhao Zhao: Center for Molecular Design and Biomimetics, the Biodesign Institute at Arizona State University
Jinglin Fu: Center for Computational and Integrative Biology, Rutgers University-Camden
Soma Dhakal: Single Molecule Analysis Group, University of Michigan
Alexander Johnson-Buck: Single Molecule Analysis Group, University of Michigan
Minghui Liu: Center for Molecular Design and Biomimetics, the Biodesign Institute at Arizona State University
Ting Zhang: Center for Computational and Integrative Biology, Rutgers University-Camden
Neal W. Woodbury: School of Molecular Sciences, Arizona State University
Yan Liu: Center for Molecular Design and Biomimetics, the Biodesign Institute at Arizona State University
Nils G. Walter: Single Molecule Analysis Group, University of Michigan
Hao Yan: Center for Molecular Design and Biomimetics, the Biodesign Institute at Arizona State University

Nature Communications, 2016, vol. 7, issue 1, 1-9

Abstract: Abstract 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.

Date: 2016
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DOI: 10.1038/ncomms10619

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