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

Jingyao Li, Bojing Jiang, Xinyuan Chang, Han Yu, Yichao Han and Fuzhong Zhang ()
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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

Nature Communications, 2023, vol. 14, issue 1, 1-12

Abstract: 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.

Date: 2023
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DOI: 10.1038/s41467-023-37563-0

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