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dc.contributor.authorFinnigan, William
dc.contributor.authorRoberts, Aled D.
dc.contributor.authorLigorio, Cosimo
dc.contributor.authorScrutton, Nigel S.
dc.contributor.authorBreitling, Rainer
dc.contributor.authorBlaker, Jonny J.
dc.contributor.authorTakano, Eriko; email: eriko.takano@manchester.ac.uk
dc.date.accessioned2021-06-30T15:36:37Z
dc.date.available2021-06-30T15:36:37Z
dc.date.issued2020-06-30
dc.date.submitted2020-02-04
dc.identifierhttps://chesterrep.openrepository.com/bitstream/handle/10034/625094/41598_2020_Article_67703.pdf?sequence=2
dc.identifierhttps://chesterrep.openrepository.com/bitstream/handle/10034/625094/additional-files.zip?sequence=3
dc.identifierhttps://chesterrep.openrepository.com/bitstream/handle/10034/625094/41598_2020_Article_67703_nlm.xml?sequence=4
dc.identifier.citationScientific Reports, volume 10, issue 1, page 10671
dc.identifier.urihttp://hdl.handle.net/10034/625094
dc.descriptionFrom Springer Nature via Jisc Publications Router
dc.descriptionHistory: received 2020-02-04, accepted 2020-06-11, registration 2020-06-15, pub-electronic 2020-06-30, online 2020-06-30, collection 2020-12
dc.descriptionPublication status: Published
dc.descriptionFunder: Defence Science and Technology Laboratory; doi: http://dx.doi.org/10.13039/100010418; Grant(s): DSTLX1000101893, DSTLX1000101893, DSTLX1000101893, DSTLX1000101893, DSTLX1000101893
dc.descriptionFunder: Engineering and Physical Sciences Research Council; doi: http://dx.doi.org/10.13039/501100000266; Grant(s): EP/L014904/1
dc.descriptionFunder: 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
dc.description.abstractAbstract: 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.
dc.languageen
dc.publisherNature Publishing Group UK
dc.rightsLicence for this article: http://creativecommons.org/licenses/by/4.0/
dc.sourceeissn: 2045-2322
dc.subjectArticle
dc.subject/631/61/252
dc.subject/639/301/54
dc.subjectarticle
dc.titleThe effect of terminal globular domains on the response of recombinant mini-spidroins to fiber spinning triggers
dc.typearticle
dc.date.updated2021-06-30T15:36:36Z
dc.date.accepted2020-06-11


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