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Silk Road Revealed: Mechanism of silk fibre formation in Bombyx mori
Open accessPreprint — 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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“It was noted before that this helix could flip out of the hydrophobic space.”
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“B) shows a high degree of orientation and is consistent both with previous Silk-I data, 14,36 and our newly proposed solenoid model.”
ResultUltrastructure of fibroin in the silk gland of larval Bombyx mori.
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“11,40 This conformation implies that in the transformation from Silk-I to Silk-II, G residues would not need to go through sterically hindered angles (see Figure S17), 41 thus reducing the overall energetic cost of the Silk-I to Silk-II transformation.”
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Artificial spinning of natural silk threads
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“It was noted before that this helix could flip out of the hydrophobic space.”
BackgroundFractionation of Regenerated Silk Fibroin and Characterization of the Fractions
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BackgroundNano-fishnet formation of silk controlled by Arginine density.
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“…Samia ricini ( Saturniid ) fibroin, 66 and recently in NSF. 67 Based on these observations and the apparent role NTD has on the reversible sol-gel transition, we propose that FibH can form high-order oligomers driven by head (NTD) interactions, making the core of the supramolecular fibre (SD.11).”
BackgroundSelf-citationRippled Sheets: The Early Polyglycine Days and Recent Developments in Nylons
Lotz, B. (2022) · ChemBioChem · doi:10.1002/cbic.202100658 · Cited by 10 · cited 1×
“29 However, the second population of torsion angles (ca. ϕ, φ = -80°, 180°) was not used to constrain the modelling and matches closely those found in the solenoidal model predicted by ColabFold as well as previously proposed angles from density functional theory (DFT) calculations.”
MethodAtomistic Simulation of Water Incorporation and Mobility in Bombyx mori Silk Fibroin
Haskew, M., Deacon, B. N., Yong, C., Hardy, J., & Murphy, S. (2021) · ACS Omega · doi:10.1021/acsomega.1c05019 · Cited by 10
Analysis of Silk I structure by X-ray and electron diffraction methods
Okuyama, K., Takanashi, K., Nakajima, Y., Hasegawa, Y., Hirabayashi, K., & Nishi, N. (1988) · doi:10.11416/kontyushigen1930.57.23 · Cited by 10 · cited 1×
“Here we observed that the protein appeared as globules with an apparent size of about 24 ±8 nm at pH 8, but elongated fibrillar structures were observed at pH 6 (SD.10).”
BackgroundSilkworm spinning: the programmed self-assembly from natural silk fibroin to superfibrePreprint
Song, K., Wang, Y., Dong, W., Li, Z., He, H., Zhu, P., & Xia, Q. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.08.434386 · Cited by 7
Takahashi, T., Miyazaki, M., Kidou, S., Matsui, Y., An, Y., Ozaki, T., Suzuki, K., & Yamashita, T. (2017) · doi:10.11416/jibs.86.3_105 · Cited by 3 · cited 2×
“B) shows a high degree of orientation and is consistent both with previous Silk-I data, 14,36 and our newly proposed solenoid model.”
MethodResult
Flagged first, then by citations
4 of the 86 references couldn’t be matched to a known paper.
Research works printed but not linked: 10
- 10.1038/s41467-021-27838-9 · DOI · Paper page
- 10.1021/ma071551d · DOI · Paper page
- 10.1101/2021.08.15.456425 · DOI · Paper page
- 10.1021/bm401346h · DOI
- 10.1186/1472-6807-5-1 · DOI
- 2012, Silk and Synthetic Polymers: Reconciling 100 Degrees of Separation, Adv. Mater, 24, 105, 10.1002/adma.201103664 · DOI
- 10.1038/s41598-019-40055-1 · DOI
- 10.1021/ACSNANO.3C00105/ASSET/IMAGES/LARGE/NN3C00105_0010.JPEG · DOI
- 10.1038/s41467-021-27838-9 · DOI · Paper page
- 10.1038/s41467-020-20241-w · DOI · Paper page
Cited by
Sorted by citations
Overview and Evolution of Insect Fibroin Heavy Chain (FibH)
Zhang, T., Ma, S., Zhang, Z., Guo, Y.-K., Yang, D., & Lu, W. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25137179 · Cited by 8
“The NTD and CTD are involved in the folding, assembly, and secretion of silk proteins, and extremely conserved across silkworm strains [9–14].”
BackgroundMoreno-Tortolero, R. O., Michalski, J., Wells, E. F., Gibb, F., Skaer, N., Walker, R., Serpell, L. C., Holland, C., & Davis, S. (2024) · Communications Materials · doi:10.1038/s43246-024-00722-x · Cited by 7
“To some extent, these experiments verify previous observations 10 , wheresilkproteinsdisplayedsmallerhydrodynamicdiameters,hence,faster diffusionratesathigherpH.”
Self-citation
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)
- PMC
- PMC11217467
- 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
- gold
- doi.org
- 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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
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