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.
journal_name
Biomacromoleculesjournal_title
Biomacromoleculesauthors
Kwak HW,Ju JE,Shin M,Holland C,Lee KHdoi
10.1021/acs.biomac.7b00549subject
Has Abstractpub_date
2017-08-14 00:00:00pages
2343-2349issue
8eissn
1525-7797issn
1526-4602journal_volume
18pub_type
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