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The effect of terminal globular domains on the response of recombinant mini-spidroins to fiber spinning triggers
Finnigan, William Roberts, Aled D. Ligorio, Cosimo Scrutton, Nigel S. Breitling, Rainer Blaker, Jonny J. Takano, Eriko; email: eriko.takano@manchester.ac.uk
Finnigan, William
Roberts, Aled D.
Ligorio, Cosimo
Scrutton, Nigel S.
Breitling, Rainer
Blaker, Jonny J.
Takano, Eriko; email: eriko.takano@manchester.ac.uk
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2020-06-30
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2020-02-04
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Abstract
Abstract: Spider silk spidroins consist of long repetitive protein strands, flanked by globular terminal domains. The globular domains are often omitted in recombinant spidroins, but are thought to be essential for the spiders’ natural spinning process. Mimicking this spinning process could be an essential step towards producing strong synthetic spider silk. Here we describe the production of a range of mini-spidroins with both terminal domains, and characterize their response to a number of biomimetic spinning triggers. Our results suggest that mini-spidroins which are able to form protein micelles due to the addition of both terminal domains exhibit shear-thinning, a property which native spidroins also show. Furthermore, our data also suggest that a pH drop alone is insufficient to trigger assembly in a wet-spinning process, and must be combined with salting-out for effective fiber formation. With these insights, we applied these assembly triggers for relatively biomimetic wet spinning. This work adds to the foundation of literature for developing improved biomimetic spinning techniques, which ought to result in synthetic silk that more closely approximates the unique properties of native spider silk.
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Scientific Reports, volume 10, issue 1, page 10671
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Nature Publishing Group UK
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article
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From Springer Nature via Jisc Publications Router
History: received 2020-02-04, accepted 2020-06-11, registration 2020-06-15, pub-electronic 2020-06-30, online 2020-06-30, collection 2020-12
Publication status: Published
Funder: Defence Science and Technology Laboratory; doi: http://dx.doi.org/10.13039/100010418; Grant(s): DSTLX1000101893, DSTLX1000101893, DSTLX1000101893, DSTLX1000101893, DSTLX1000101893
Funder: Engineering and Physical Sciences Research Council; doi: http://dx.doi.org/10.13039/501100000266; Grant(s): EP/L014904/1
Funder: Biotechnology and Biological Sciences Research Council; doi: http://dx.doi.org/10.13039/501100000268; Grant(s): BB/M017702/1, BB/M017702/1, BB/M017702/1
History: received 2020-02-04, accepted 2020-06-11, registration 2020-06-15, pub-electronic 2020-06-30, online 2020-06-30, collection 2020-12
Publication status: Published
Funder: Defence Science and Technology Laboratory; doi: http://dx.doi.org/10.13039/100010418; Grant(s): DSTLX1000101893, DSTLX1000101893, DSTLX1000101893, DSTLX1000101893, DSTLX1000101893
Funder: Engineering and Physical Sciences Research Council; doi: http://dx.doi.org/10.13039/501100000266; Grant(s): EP/L014904/1
Funder: Biotechnology and Biological Sciences Research Council; doi: http://dx.doi.org/10.13039/501100000268; Grant(s): BB/M017702/1, BB/M017702/1, BB/M017702/1