ArticleJournal of the Royal Society, Interface2014
On the strength of β-sheet crystallites of Bombyx mori silk fibroin.
Article in Journal of the Royal Society, Interface, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed.
- Structural and immunogenic evaluation of silk proteins from Bombyx mori using advanced bioinformatics and deep learning for biomaterials applications.Journal, genetic engineering & biotechnology · 2026Article
- Recent Advances in Silk Fibroin Derived fromJournal of functional biomaterials · 2025Review
- Silk Fibroin Protective Coating for Washable and Reusable Textile Electronics.International journal of molecular sciences · 2025Article
- Chitin nanofibers: recent advances in preparation and applications in biomedical and beyond.RSC advances · 2025Review
- Elasticity Anisotropy ofBiomacromolecules · 2025Article
- Article
- Design and applications of self-assembled polypeptide matrices in wound healing.Frontiers in bioengineering and biotechnology · 2025Review
- The Impact of Temperature and Pressure on the Structural Stability of Solvated Solid-State Conformations ofMaterials (Basel, Switzerland) · 2024Article
- Progress in Multiscale Modeling of Silk Materials.Biomacromolecules · 2024Review
- Comparative Analysis of Silk Fibroin Membranes across Cross-Linking Methods: Processing and Characterization.ACS omega · 2024Article
- Silk Fibroin-Enriched Bioink Promotes Cell Proliferation in 3D-Bioprinted Constructs.Gels (Basel, Switzerland) · 2024Article
- Tailoring silk fibroin hydrophilicity and physicochemical properties using sugar alcohols for medical device coatings.Scientific reports · 2024Article
- Stepwise degradable PGA-SF core-shell electrospinning scaffold with superior tenacity in wetting regime for promoting bone regeneration.Materials today. Bio · 2024Article
- Review
- Tuning the Topography of Dynamic 3D Scaffolds through Functional Protein Wrinkled Coatings.Polymers · 2024Article
- A facile nanopattern modification of silk fibroin electrospun scaffold and the corresponding impact on cell proliferation and osteogenesis.Regenerative biomaterials · 2024Article
- Versatile Potential of Photo-Cross-Linkable Silk Fibroin: Roadmap from Chemical Processing Toward Regenerative Medicine and Biofabrication Applications.Biomacromolecules · 2023Review
- Article
- Advances in Hydrogel Adhesives for Gastrointestinal Wound Closure and Repair.Gels (Basel, Switzerland) · 2023Review
- Controllable Production of Natural Silk Nanofibrils for Reinforcing Silk-Based Orthopedic Screws.Polymers · 2023Article
Corrections and comments
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Authors and funding
6 authors.
Funding
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Abstract
Silk fibroin, a natural multi-domain protein, has attracted great attention due to its superior mechanical properties such as ultra-high strength and stretchability, biocompatibility, as well as its versatile biodegradability and processability. It is mainly composed of β-sheet crystallites and amorphous domains. Although its strength is well known to be controlled by the dissociation of protein chains from β-sheet crystallites, the way that water as the solvent affects its strength and the reason that its theoretically predicted strength is several times higher than experimental measurement remain unclear. We perform all-atom molecular dynamics simulations on a β-sheet crystallite of Bombyx mori silk. We find that water solvent reduces the number and strength of hydrogen bonds between β-chains, and thus greatly weakens the strength of silk fibroin. By dissociating protein chains at different locations from the crystallite, we also find that the pulling strength for the interior chains is several times higher than that for the surface/corner chains, with the former being consistent with the theoretically predicted value, while the latter on par with the experimental value. It is shown that the weakest rupture strength controls the failure strength of silk fibre. Hence, this work sheds light on the role of water in the strength of silk fibroin and also provides clues on the origin of the strength difference between theory and experiment.
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