Projects per year
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.
Original language | English |
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Article number | e4907 |
Number of pages | 8 |
Journal | Protein Science |
Volume | 33 |
Issue number | 3 |
DOIs | |
Publication status | Published - Mar 2024 |
MoE publication type | A1 Journal article-refereed |
Keywords
- amino acid analysis
- Bombyx mori
- fibroin
- middle silk gland
- sericin
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LIBER Linder: Life-like hybrid materials
Linder, M. (Principal investigator)
01/01/2022 → 31/12/2026
Project: Academy of Finland: Other research funding
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CATBAT: A combinatorial approach towards biological materials
Linder, M. (Principal investigator)
01/05/2020 → 30/04/2025
Project: Other external funding: Other foreign funding
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AI spider silk threading
Linder, M. (Principal investigator)
01/01/2018 → 31/12/2021
Project: Academy of Finland: Other research funding