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Spidroin N-terminal domain forms amyloid-like fibril based hydrogels and provides a protein immobilization platform

Author

Listed:
  • Tina Arndt

    (Karolinska Institutet, Neo)

  • Kristaps Jaudzems

    (Latvian Institute of Organic Synthesis)

  • Olga Shilkova

    (Karolinska Institutet, Neo)

  • Juanita Francis

    (Karolinska Institutet, Neo)

  • Mathias Johansson

    (Swedish University of Agricultural Sciences)

  • Peter R. Laity

    (The University of Sheffield)

  • Cagla Sahin

    (Karolinska Institutet)

  • Urmimala Chatterjee

    (Karolinska Institutet, Neo)

  • Nina Kronqvist

    (Karolinska Institutet, Neo)

  • Edgar Barajas-Ledesma

    (Karolinska Institutet)

  • Rakesh Kumar

    (Karolinska Institutet, Neo)

  • Gefei Chen

    (Karolinska Institutet, Neo)

  • Roger Strömberg

    (Karolinska Institutet, Neo)

  • Axel Abelein

    (Karolinska Institutet, Neo)

  • Maud Langton

    (Swedish University of Agricultural Sciences)

  • Michael Landreh

    (Karolinska Institutet)

  • Andreas Barth

    (Stockholm University)

  • Chris Holland

    (The University of Sheffield)

  • Jan Johansson

    (Karolinska Institutet, Neo)

  • Anna Rising

    (Karolinska Institutet, Neo
    Swedish University of Agricultural Sciences)

Abstract

Recombinant spider silk proteins (spidroins) have multiple potential applications in development of novel biomaterials, but their multimodal and aggregation-prone nature have complicated production and straightforward applications. Here, we report that recombinant miniature spidroins, and importantly also the N-terminal domain (NT) on its own, rapidly form self-supporting and transparent hydrogels at 37 °C. The gelation is caused by NT α-helix to β-sheet conversion and formation of amyloid-like fibrils, and fusion proteins composed of NT and green fluorescent protein or purine nucleoside phosphorylase form hydrogels with intact functions of the fusion moieties. Our findings demonstrate that recombinant NT and fusion proteins give high expression yields and bestow attractive properties to hydrogels, e.g., transparency, cross-linker free gelation and straightforward immobilization of active proteins at high density.

Suggested Citation

  • Tina Arndt & Kristaps Jaudzems & Olga Shilkova & Juanita Francis & Mathias Johansson & Peter R. Laity & Cagla Sahin & Urmimala Chatterjee & Nina Kronqvist & Edgar Barajas-Ledesma & Rakesh Kumar & Gefe, 2022. "Spidroin N-terminal domain forms amyloid-like fibril based hydrogels and provides a protein immobilization platform," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
  • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-32093-7
    DOI: 10.1038/s41467-022-32093-7
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    References listed on IDEAS

    as
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    2. Franz Hagn & Lukas Eisoldt & John G. Hardy & Charlotte Vendrely & Murray Coles & Thomas Scheibel & Horst Kessler, 2010. "A conserved spider silk domain acts as a molecular switch that controls fibre assembly," Nature, Nature, vol. 465(7295), pages 239-242, May.
    3. Nina Kronqvist & Martins Otikovs & Volodymyr Chmyrov & Gefei Chen & Marlene Andersson & Kerstin Nordling & Michael Landreh & Médoune Sarr & Hans Jörnvall & Stefan Wennmalm & Jerker Widengren & Qing Me, 2014. "Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formation," Nature Communications, Nature, vol. 5(1), pages 1-11, May.
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