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Chemical, Thermal, Time, and Enzymatic Stability of Silk Materials with Silk I Structure
Open accessAbstract
The crystalline structure of silk fibroin Silk I is generally considered to be a metastable structure; however, there is no definite conclusion under what circumstances this crystalline structure is stable or the crystal form will change. In this study, silk fibroin solution was prepared from B. Mori silkworm cocoons, and a combined method of freeze-crystallization and freeze-drying at different temperatures was used to obtain stable Silk I crystalline material and uncrystallized silk material, respectively. Different concentrations of methanol and ethanol were used to soak the two materials with different time periods to investigate the effect of immersion treatments on the crystalline structure of silk fibroin materials. X-ray diffraction (XRD), Fourier transform infrared spectroscopy (FTIR), Raman scattering spectroscopy (Raman), Scanning electron microscope (SEM), and Thermogravimetric analysis (TGA) were used to characterize the structure of silk fibroin before and after the treatments. The results showed that, after immersion treatments, uncrystallized silk fibroin material with random coil structure was transformed into Silk II crystal structure, while the silk material with dominated Silk I crystal structure showed good long-term stability without obvious transition to Silk II crystal structure. α-chymotrypsin biodegradation study showed that the crystalline structure of silk fibroin Silk I materials is enzymatically degradable with a much lower rate compared to uncrystallized silk materials. The crystalline structure of Silk I materials demonstrate a good long-term stability, endurance to alcohol sterilization without structural changes, and can be applied to many emerging fields, such as biomedical materials, sustainable materials, and biosensors.
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“The principal thermal degradation event for SF and SFMA occurred at 293.0 and 292.0 °C, respectively, corresponding to the breakdown of the protein backbone and the degradation of both amorphous regions and β-sheet crystalline domains [55].”
From Montmorillonite-reinforced methacrylated collagen/methacrylated silk fibroin hydrogel-based inks: rheological and physicochemical characterization for bone scaffold applications (2026) · cites this paper as [55]
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Metadata
- Authors
- Zhao, M., Qi, Z., Tao, X., Newkirk, C., Hu, X., & Lu, S.
- Affiliations
- Soochow University (CN)
- Rowan University (US)
- Corresponding author
- Hu, Xiao
- Lu, Shenzhou
- ORCID
- Venue
- International Journal of Molecular Sciences
- Publisher
- MDPI AG
- Published
- 2021-04-16
- Volume
- 22
- Issue
- 8
- Pages
- 4136
- ISSN
- 1422-0067 (ISSN-L)
- PMC
- PMC8073524
- OpenAlex
- W3153480078
- Cited by
- 130
- References
- 32
- Citations by year
- 2026: 36 · 2025: 34 · 2024: 24 · 2023: 18 · 2022: 16 · 2021: 2
- FWCI
- 3.92
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- International Journal of Molecular Sciences (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Rowan Digitals Works (Rowan University) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Natural Science Foundation of China (51973144)
- Six Talent Peaks Project in Jiangsu Province (SWYY-038)
- College Nature Science Research Project of Jiangsu Province (20KJA540002)
- US Natural Science Foundation Biomaterials Program (DMR-1809541)
- 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 › Polymers and Plastics › Dyeing and Modifying Textile Fibers
- Keywords
- silk fibroin, freeze crystallization, freeze-drying, random coil, enzymatic degradation, thermal stability, chemical stability, Bombyx mori
- MeSH terms
- Chymotrypsin, Fibroins, Hot Temperature, Protein Denaturation, Protein Stability, Proteolysis
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