Degradation mechanism and control of silk fibroin
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Controlling the degradation process of silk is an important and interesting subject in the field of biomaterials. In the present study, silk fibroin films with different secondary conformations and nanostructures were used to study degradation behavior in buffered protease XIV solution. Different from previous studies, silk fibroin films with highest β-sheet content achieved the highest degradation rate in our research. A new degradation mechanism revealed that degradation behavior of silk fibroin was related to not only crystal content but also hydrophilic interaction and then crystal-noncrystal alternate nanostructures. First, hydrophilic blocks of silk fibroin were degraded. Then, hydrophobic crystal blocks that were formerly surrounded and immobilized by hydrophilic blocks became free particles and moved into solution. Therefore, on the basis of the mechanism, which enables the process to be more controllable and flexible, controlling the degradation behavior of silk fibroin without affecting other performances such as its mechanical or hydrophilic properties becomes feasible, and this would greatly expand the applications of silk as a biomedical material.
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A further transition in SF at approximately 287.0 °C corresponds to extensive energetic disruption of highly ordered intermolecular interactions within the β-sheet dominated structure, marking an advanced stage of thermal destabilization of silk fibroin.
“At higher temperatures, a further transition observed at approximately 287.0 °C corresponds to extensive energetic disruption of highly ordered intermolecular interactions within the β-sheet dominated structure, marking an advanced stage of thermal destabilization of the silk fibroin [47].”
From Montmorillonite-reinforced methacrylated collagen/methacrylated silk fibroin hydrogel-based inks: rheological and physicochemical characterization for bone scaffold applications (2026) · cites this paper as [47]
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- Authors
- Lu, Q., Zhang, B., Li, M., Zuo, B., Kaplan, D. L., Huang, Y., & Zhu, H.
- Affiliations
- National Engineering Laboratory for Modern Silk, College of Textile and Clothing Engineering, Soochow University, Suzhou 215123, People’s Republic of China
- Soochow University (CN)
- Tufts University (US)
- Beijing Institute of Technology (CN)
- Venue
- Biomacromolecules
- Publisher
- American Chemical Society (ACS)
- Published
- 2011-02-25
- Volume
- 12
- Issue
- 4
- Pages
- 1080-1086
- ISSN
- 1525-7797 (ISSN-L)
- 1526-4602
- PMC
- PMC3404841
- OpenAlex
- W2035560364
- Cited by
- 344
- References
- 38
- Citations by year
- 2026: 35 · 2025: 25 · 2024: 23 · 2023: 18 · 2022: 26 · 2021: 29 · 2020: 34 · 2019: 33 · 2018: 18 · 2017: 17 · 2016: 21 · 2015: 16 · 2014: 23 · 2013: 11 · 2012: 12
- FWCI
- 6.43
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Biomacromolecules (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Natural Science Foundation of China
- National Institutes of Health
- National Institute of Biomedical Imaging and Bioengineering (EB-002520, P41EB002520)
- Topics
- Physical Sciences › Materials Science › Biomaterials › Silk-based biomaterials and applications
- Physical Sciences › Materials Science › Biomaterials › biodegradable polymer synthesis and properties
- Life Sciences › Agricultural and Biological Sciences › Insect Science › Silkworms and Sericulture Research
- Keywords
- silk fibroin, degradation mechanism, silk fibroin films, β-sheet content, secondary structure, protease XIV, hydrophobic-hydrophilic interactions, controlled degradation, biomaterials
- MeSH terms
- Calorimetry, Differential Scanning, Fibroins, Hydrolysis, Solutions, Spectroscopy, Fourier Transform Infrared, Microscopy, Atomic Force, Silk
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