PreprintCited by 45Silk-based biomaterials and applicationsSilkworms and Sericulture ResearchSupramolecular Self-Assembly in Materials

The DOI matches its Crossref record; 82 of the 86 references it cites were found in a registry or an index.

Silk Road Revealed: Mechanism of silk fibre formation in Bombyx mori

Open access
Moreno-Tortolero, R.O., Luo, Y., Parmeggiani, F., Skaer, N., Walker, R., Serpell, L., Holland, C., Davis, S.A.·2023·Communications Biology

Preprint — published as 10.1038/s42003-024-06474-1 · Paper page

Abstract

The transition of silk fibroin from liquid to solid is fundamental to silk-fibre production and key to the superior materials properties of native silks. Here we discover that the fibroin heavy chain from the silkworm moth Bombyx mori folds into a novel β-solenoid structure, where the N-terminal domain (NTD) promotes higher-order oligomerization driven by pH reduction. These findings elucidate the complex rheological behaviour of silk and the liquid crystalline textures within the silk gland. We also find that NTD undergoes hydrolysis during standard regeneration, explaining differences between native and regenerated silk feedstocks. Overall, this study establishes a fibroin heavy chain fold, which could be relevant for other similar proteins, and explains mechanistically its liquid-to-solid transition, driven by pH reduction and stress. One sentence summary: This study redefines the molecular structure of fibroin heavy chain and its role in the transition from solution to fibre.

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Crossref · 10.1101/2023.06.02.543394

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Research works printed but not linked: 10

  1. 10.1038/s41467-021-27838-9 · DOI · Paper page
  2. 10.1021/ma071551d · DOI · Paper page
  3. 10.1101/2021.08.15.456425 · DOI · Paper page
  4. 10.1021/bm401346h · DOI
  5. 10.1186/1472-6807-5-1 · DOI
  6. 2012, Silk and Synthetic Polymers: Reconciling 100 Degrees of Separation, Adv. Mater, 24, 105, 10.1002/adma.201103664 · DOI
  7. 10.1038/s41598-019-40055-1 · DOI
  8. 10.1021/ACSNANO.3C00105/ASSET/IMAGES/LARGE/NN3C00105_0010.JPEG · DOI
  9. 10.1038/s41467-021-27838-9 · DOI · Paper page
  10. 10.1038/s41467-020-20241-w · DOI · Paper page

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Metadata

Authors
Moreno-Tortolero, R. O., Luo, Y., Parmeggiani, F., Skaer, N., Walker, R., Serpell, L., Holland, C., & Davis, S. A.
Affiliations
  • University of Bristol (GB)
  • Orthox (United Kingdom) (GB)
  • University of Sussex (GB)
  • University of Sheffield (GB)
Corresponding author
Davis, S.A.
Venue
Communications Biology
Publisher
openRxiv
Published
2023-06-03
Volume
7
Issue
1
Pages
786-786
ISSN
2399-3642 (ISSN-L)
OpenAlex
W4400198937
Cited by
45
References
86
Citations by year
2026: 23 · 2025: 14 · 2024: 7 · 2023: 1
FWCI
4.14
Type
journal article
Language
en
Open access
Licence
cc-by
Locations
  • Communications Biology (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Bristol Research (University of Bristol) (publishedVersion, cc-by)
  • White Rose Research Online (University of Leeds, The University of Sheffield, University of York) (acceptedVersion, cc-by)
  • Figshare (submittedVersion, cc-by)
  • ORCA Online Research @Cardiff (Cardiff University) (submittedVersion, cc-by)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
  • Explore Bristol Research (submittedVersion, cc-by)
  • Bristol Research (University of Bristol) (submittedVersion, cc-by-nc-nd)
Funders
  • Wellcome Trust (206181/Z/17/Z, Z/17/Z, 086906/Z/08/Z, 202904/Z/16/Z, 100917/Z/13/Z)
  • National Institute for Health and Care Research (II-LB-0417-20005)
  • Department of Health and Social Care
  • University of Bristol (BB/L01386X/1, EP/K035746/1)
  • China Scholarship Council
  • Engineering and Physical Sciences Research Council (EP/M028216/1, EP/W524414/1, (BB/L01386X/1), EP/S017542/1, EP/K035746/1, BB/L01386X, EP/X015416/1, L01386X)
  • Biotechnology and Biological Sciences Research Council (BB/L01386X/1, BB/L01386X, BB/R000484/1, BB/V019163/1, L01386X)
  • Invention for Innovation
  • BrisSynBio (BB/L01386X/1)
Topics
  • Physical Sciences › Materials Science › Biomaterials › Silk-based biomaterials and applications
  • Life Sciences › Agricultural and Biological Sciences › Insect Science › Silkworms and Sericulture Research
  • Physical Sciences › Materials Science › Biomaterials › Supramolecular Self-Assembly in Materials
Keywords
fibroin heavy chain, Bombyx mori, solidification, N-terminal domain, silk gland, protein self-assembly
MeSH terms
Animals, Fibroins, Hydrogen-Ion Concentration, Rheology, Bombyx, Silk

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