IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v4y2013i1d10.1038_ncomms3211.html
   My bibliography  Save this article

Hyperthin nanochains composed of self-polymerizing protein shackles

Author

Listed:
  • Ryo Matsunaga

    (The Medical Proteomics Laboratory, The Institute of Medical Science, The University of Tokyo
    Graduate School of Frontier Sciences, The University of Tokyo)

  • Saeko Yanaka

    (The Medical Proteomics Laboratory, The Institute of Medical Science, The University of Tokyo
    Graduate School of Frontier Sciences, The University of Tokyo)

  • Satoru Nagatoishi

    (The Medical Proteomics Laboratory, The Institute of Medical Science, The University of Tokyo
    Graduate School of Engineering, The University of Tokyo)

  • Kouhei Tsumoto

    (The Medical Proteomics Laboratory, The Institute of Medical Science, The University of Tokyo
    Graduate School of Frontier Sciences, The University of Tokyo
    Graduate School of Engineering, The University of Tokyo
    Graduate School of Engineering, The University of Tokyo)

Abstract

Protein fibrils are expected to have applications as functional nanomaterials because of their sophisticated structures; however, nanoscale ordering of the functional units of protein fibrils remains challenging. Here we design a series of self-polymerizing protein monomers, referred to as protein shackles, derived from modified recombinant subunits of pili from Streptococcus pyogenes. The monomers polymerize into nanochains through spontaneous irreversible covalent bond formation. We design the protein shackles so that their reactions can be controlled by altering redox conditions, which affect disulphide bond formation between engineered cysteine residues. The interaction between the monomers improves their polymerization reactivity and determines morphologies of the polymers. In addition, green fluorescent protein-tagged protein shackles can polymerize, indicating proteins can be stably attached to the nanochains with its functionality preserved. Furthermore we demonstrate that a molecular-recognizable nanochain binds to its partner with an enhanced binding ability in solution. These characteristics are expected to be applied for novel protein nanomaterials.

Suggested Citation

  • Ryo Matsunaga & Saeko Yanaka & Satoru Nagatoishi & Kouhei Tsumoto, 2013. "Hyperthin nanochains composed of self-polymerizing protein shackles," Nature Communications, Nature, vol. 4(1), pages 1-10, October.
    • Handle: RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms3211
    DOI: 10.1038/ncomms3211
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/ncomms3211
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/ncomms3211?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. Christian Hentrich & Mateusz Putyrski & Hanh Hanuschka & Waldemar Preis & Sarah-Jane Kellmann & Melissa Wich & Manuel Cavada & Sarah Hanselka & Victor S. Lelyveld & Francisco Ylera, 2024. "Engineered reversible inhibition of SpyCatcher reactivity enables rapid generation of bispecific antibodies," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    2. Claudia L. Driscoll & Anthony H. Keeble & Mark R. Howarth, 2024. "SpyMask enables combinatorial assembly of bispecific binders," Nature Communications, Nature, vol. 15(1), pages 1-17, December.
    3. Susan K. Vester & Rolle Rahikainen & Irsyad N. A. Khairil Anuar & Rory A. Hills & Tiong Kit Tan & Mark Howarth, 2022. "SpySwitch enables pH- or heat-responsive capture and release for plug-and-display nanoassembly," Nature Communications, Nature, vol. 13(1), pages 1-16, 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:4:y:2013:i:1:d:10.1038_ncomms3211. 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.