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  Artificial hagfish protein fibers with ultra-high and tunable stiffness

Fu, J., Guerette, P. A., Pavesi, A., Horbelt, N., Lim, C. T., Harrington, M. J., et al. (2017). Artificial hagfish protein fibers with ultra-high and tunable stiffness. Nanoscale, 9(35), 12908-12915. doi:10.1039/C7NR02527K.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-17A7-7 Version Permalink: http://hdl.handle.net/21.11116/0000-0007-04AA-5
Genre: Journal Article

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 Creators:
Fu, Jing, Author
Guerette, Paul A., Author
Pavesi, Andrea, Author
Horbelt, Nils1, Author              
Lim, Chwee Teck, Author
Harrington, Matthew J.1, Author              
Miserez, Ali, Author
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1Matthew Harrington, Biomaterialien, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863292              

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 Abstract: Stiff fibers are used as reinforcing phases in a wide range of high-performance composite materials. Silk is one of the most widely studied bio-fibers, but alternative materials with specific advantages are also being explored. Among these, native hagfish (Eptatretus stoutii) slime thread is an attractive protein-based polymer. These threads consist of coiled-coil intermediate filaments (IFs) as nano-scale building blocks, which can be transformed into extended [small beta]-sheet-containing chains upon draw-processing, resulting in fibers with impressive mechanical performance. Here, we report artificial hagfish threads produced by recombinant protein expression, which were subsequently self-assembled into coiled-coil nanofilaments, concentrated, and processed into [small beta]-sheet-rich fibers by a "picking-up" method. These artificial fibers experienced mechanical performance enhancement during draw-processing. We exploited the lysine content to covalently cross-link the draw-processed fibers and obtained moduli values (E) in tension as high as [similar]20 GPa, which is stiffer than most reported artificial proteinaceous materials.

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 Dates: 2017-09-21
 Publication Status: Published in print
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 Identifiers: DOI: 10.1039/C7NR02527K
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Title: Nanoscale
Source Genre: Journal
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Publ. Info: Cambridge, UK : Royal Society of Chemistry
Pages: - Volume / Issue: 9 (35) Sequence Number: - Start / End Page: 12908 - 12915 Identifier: ISSN: 2040-3364