IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v7y2016i1d10.1038_ncomms10619.html
   My bibliography  Save this article

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

Author

Listed:
  • Zhao Zhao

    (Center for Molecular Design and Biomimetics, the Biodesign Institute at Arizona State University
    School of Molecular Sciences, 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
    Center for Innovations in Medicine, the Biodesign Institute at Arizona State University)

  • Yan Liu

    (Center for Molecular Design and Biomimetics, the Biodesign Institute at Arizona State University
    School of Molecular Sciences, 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
    School of Molecular Sciences, Arizona State University)

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.

Suggested Citation

  • Zhao Zhao & Jinglin Fu & Soma Dhakal & Alexander Johnson-Buck & Minghui Liu & Ting Zhang & Neal W. Woodbury & Yan Liu & Nils G. Walter & Hao Yan, 2016. "Nanocaged enzymes with enhanced catalytic activity and increased stability against protease digestion," Nature Communications, Nature, vol. 7(1), pages 1-9, April.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms10619
    DOI: 10.1038/ncomms10619
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/ncomms10619
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/ncomms10619?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Yuhao Weng & Huihong Chen & Xiaoqian Chen & Huilin Yang & Chia-Hung Chen & Hongliang Tan, 2022. "Adenosine triphosphate-activated prodrug system for on-demand bacterial inactivation and wound disinfection," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    2. Vishal Maingi & Zhao Zhang & Chris Thachuk & Namita Sarraf & Edwin R. Chapman & Paul W. K. Rothemund, 2023. "Digital nanoreactors to control absolute stoichiometry and spatiotemporal behavior of DNA receptors within lipid bilayers," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    3. Jing Mu & Chunxiao Li & Yu Shi & Guoyong Liu & Jianhua Zou & Dong-Yang Zhang & Chao Jiang & Xiuli Wang & Liangcan He & Peng Huang & Yuxin Yin & Xiaoyuan Chen, 2022. "Protective effect of platinum nano-antioxidant and nitric oxide against hepatic ischemia-reperfusion injury," Nature Communications, Nature, vol. 13(1), pages 1-12, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms10619. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.