ArticleProtein science : a publication of the Protein Society2024
The ratio of fibroin to sericin in the middle silk gland of Bombyx mori and its correlation with the extensional behavior of the silk dope.
Article in Protein science : a publication of the Protein Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 9 citations in OpenAlex.
- Structural and immunogenic evaluation of silk proteins from Bombyx mori using advanced bioinformatics and deep learning for biomaterials applications.Journal, genetic engineering & biotechnology · 2026Article
- Silver Nanoparticle-Silk Protein Nanocomposites: A Synergistic Biomimetic Approach for Advanced Antimicrobial Applications.Biomimetics (Basel, Switzerland) · 2025Review
- Silk Protein Gene Engineering and Its Applications: Recent Advances in Biomedicine Driven by Molecular Biotechnology.Drug design, development and therapy · 2025Review
- Photobonding of silk fibroin-based hydrogels to rabbit corneas.Frontiers in bioengineering and biotechnology · 2025Article
- The ratio of fibroin to sericin in the middle silk gland of Bombyx mori and its correlation with the extensional behavior of the silk dope.Protein science : a publication of the Protein Society · 2024Article
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2 authors at 1 institution in 1 country.
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Abstract
Understanding how native silk spinning occurs is crucial for designing artificial spinning systems. One often overlooked factor in Bombyx mori is the secretion of sericin proteins. Herein, we investigate the variation in amino acid content at different locations in the middle silk gland (MSG) of B. mori. This variation corresponds to an increase in sericin content when moving towards the anterior region of the MSG, while the posterior region predominantly contains fibroin. We estimate the mass ratio of sericin to fibroin to be ~25/75 wt% in the anterior MSG, depending on the fitting method. Then, we demonstrate that the improvement in the extensional behavior of the silk dope in the MSG correlates with the increase in sericin content. The addition of sericin may decrease the viscosity of the silk dope, a factor associated with an increase in the spinnability of silk. We further discuss whether this effect could also result from other known physicochemical changes within the MSG.
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