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Bi-terminal fusion of intrinsically-disordered mussel foot protein fragments boosts mechanical strength for protein fibers

Author

Listed:
  • Jingyao Li

    (Washington University in St. Louis)

  • Bojing Jiang

    (Washington University in St. Louis)

  • Xinyuan Chang

    (Washington University in St. Louis)

  • Han Yu

    (Washington University in St. Louis)

  • Yichao Han

    (Washington University in St. Louis)

  • Fuzhong Zhang

    (Washington University in St. Louis
    Washington University in St. Louis
    Washington University in St. Louis)

Abstract

Microbially-synthesized protein-based materials are attractive replacements for petroleum-derived synthetic polymers. However, the high molecular weight, high repetitiveness, and highly-biased amino acid composition of high-performance protein-based materials have restricted their production and widespread use. Here we present a general strategy for enhancing both strength and toughness of low-molecular-weight protein-based materials by fusing intrinsically-disordered mussel foot protein fragments to their termini, thereby promoting end-to-end protein-protein interactions. We demonstrate that fibers of a ~60 kDa bi-terminally fused amyloid-silk protein exhibit ultimate tensile strength up to 481 ± 31 MPa and toughness of 179 ± 39 MJ*m−3, while achieving a high titer of 8.0 ± 0.70 g/L by bioreactor production. We show that bi-terminal fusion of Mfp5 fragments significantly enhances the alignment of β-nanocrystals, and intermolecular interactions are promoted by cation-π and π-π interactions between terminal fragments. Our approach highlights the advantage of self-interacting intrinsically-disordered proteins in enhancing material mechanical properties and can be applied to a wide range of protein-based materials.

Suggested Citation

  • Jingyao Li & Bojing Jiang & Xinyuan Chang & Han Yu & Yichao Han & Fuzhong Zhang, 2023. "Bi-terminal fusion of intrinsically-disordered mussel foot protein fragments boosts mechanical strength for protein fibers," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
  • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-37563-0
    DOI: 10.1038/s41467-023-37563-0
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    References listed on IDEAS

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    1. Glareh Askarieh & My Hedhammar & Kerstin Nordling & Alejandra Saenz & Cristina Casals & Anna Rising & Jan Johansson & Stefan D. Knight, 2010. "Self-assembly of spider silk proteins is controlled by a pH-sensitive relay," Nature, Nature, vol. 465(7295), pages 236-238, May.
    2. Wenqin Bai & Cameron J. Sargent & Jeong-Mo Choi & Rohit V. Pappu & Fuzhong Zhang, 2019. "Covalently-assembled single-chain protein nanostructures with ultra-high stability," Nature Communications, Nature, vol. 10(1), pages 1-10, December.
    3. 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.
    4. Christopher H. Bowen & Cameron J. Sargent & Ao Wang & Yaguang Zhu & Xinyuan Chang & Jingyao Li & Xinyue Mu & Jonathan M. Galazka & Young-Shin Jun & Sinan Keten & Fuzhong Zhang, 2021. "Microbial production of megadalton titin yields fibers with advantageous mechanical properties," Nature Communications, Nature, vol. 12(1), pages 1-12, December.
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