Kwak, H.W., Ju, J.E., Shin, M. et al. (2 more authors) (2017) Sericin promotes fibroin silk I stabilization across a phase-separation. Biomacromolecules, 18 (8). pp. 2343-2349. ISSN 1525-7797
Abstract
Natural silk spinning offers several advantages over the synthetic fiber spinning, although the underlying mechanisms of this process are yet to be fully elucidated. Silkworm silks, specifically B. mori, comprise two main proteins: fibroin, which forms the fiber, and sericin, a coextruded coating that acts as a matrix in the resulting nonwoven composite cocoon. To date, most studies have focused on fibroin's self-assembly and gelation, with the influence of sericin during spinning receiving little to no attention. This study investigates sericin's effects on the self-assembly of fibroin via their natural phase-separation. Through changes in sample opacity, FTIR, and XRD, we report that increasing sericin concentration retards the time to gelation and β-sheet formation of fibroin, causing it to adopt a Silk I conformation. Such findings have important implications for both the natural silk spinning process and any future industrial applications, suggesting that sericin may be able to induce long-range conformational and stability control in silk fibroin, while being in a separate phase, a factor that would facilitate long-term storage or silk feedstocks.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2017 American Chemical Society. This is an open access article published under a Creative Commons Attribution (CC-BY) License, which permits unrestricted use, distribution and reproduction in any medium, provided the author and source are cited. |
Keywords: | Silk fibroin; Silk sericin; Phase-separation; Silk I structure; Gelation |
Dates: |
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Institution: | The University of Sheffield |
Academic Units: | The University of Sheffield > Faculty of Engineering (Sheffield) > Department of Materials Science and Engineering (Sheffield) |
Depositing User: | Symplectic Sheffield |
Date Deposited: | 13 Jul 2017 12:08 |
Last Modified: | 18 Aug 2023 11:10 |
Status: | Published |
Publisher: | American Chemical Society |
Refereed: | Yes |
Identification Number: | 10.1021/acs.biomac.7b00549 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:119005 |
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