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

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Molecular organization of fibroin heavy chain and mechanism of fibre formation in Bombyx mori

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Moreno-Tortolero, Rafael O., Luo, Yijie, Parmeggiani, Fabio, Skaer, Nick, Walker, Robert, Serpell, Louise C., Holland, Chris, Davis, Sean A.·2024·Communications Biology
DOI 10.1038/s42003-024-06474-1PMC PMC11217467

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Abstract

Fibroins’ transition from liquid to solid is fundamental to spinning and underpins the impressive native properties of silk. Herein, we establish a fibroin heavy chain fold for the Silk-I polymorph, which could be relevant for other similar proteins, and explains mechanistically the liquid-to-solid transition of this silk, driven by pH reduction and flow stress. Combining spectroscopy and modelling we propose that the liquid Silk-I fibroin heavy chain (FibH) from the silkworm, Bombyx mori , adopts a newly reported β-solenoid structure. Similarly, using rheology we propose that FibH N-terminal domain (NTD) templates reversible higher-order oligomerization driven by pH reduction. Our integrated approach bridges the gap in understanding FibH structure and provides insight into the spatial and temporal hierarchical self-assembly across length scales. Our findings elucidate the complex rheological behaviour of Silk-I, solutions and gels, and the observed liquid crystalline textures within the silk gland. We also find that the NTD undergoes hydrolysis during standard regeneration, explaining key differences between native and regenerated silk feedstocks. In general, in this study we emphasize the unique characteristics of native and native-like silks, offering a fresh perspective on our fundamental understanding of silk-fibre production and applications.

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Metadata

Authors
Moreno-Tortolero, R. O., Luo, Y., Parmeggiani, F., Skaer, N., Walker, R., Serpell, L. C., 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, Sean A.
ORCID
Venue
Communications Biology
Publisher
Springer Science and Business Media LLC
Published
2024-06-29
Volume
7
Issue
1
Pages
786-786
ISSN
2399-3642 (ISSN-L)
DOI
10.1038/s42003-024-06474-1
PMC
PMC11217467
OpenAlex
W4400198937
Cited by
45
References
5
Citations by year
2026: 23 · 2025: 14 · 2024: 7
FWCI
4.11
Type
journal article
Language
en
Open access
Licence
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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