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Lithium-free processing of silk fibroin
Abstract
Silk fibroin protein was purified from Bombyx mori silkworm cocoons using a novel dialysis strategy to avoid fibroin aggregation and pre-mature formation of β-sheets. The degummed silk fibers were dissolved in Ajisawa's reagent, a mixture of CaCl2-EtOH-H2O, that is less expensive than lithium bromide. The dissolved solutions were dialyzed against either water or urea solution with a stepwise decrease in concentration. When the steps of 4 M-2 M-1 M-0 M urea (referred to as silk-TS-4210) were adopted, the purified silk fibroin had smaller aggregates (<10 nm), similar average molecular weight (225 kDa) and a lower content of β-sheet (∼15%) compared to the sample processing methods (silk-TS-210, 10, 0) studied here. This outcome was close to the fibroin purified by the lithium bromide (silk-Li-0) method. Polyvinyl alcohol-emulsified silk microspheres generated using the purified solution had a similar size distribution and morphology when compared to lithium bromide dissolved solutions, while glycerol-blended silk films showed different mechanical properties. The silk-Li-0 generated films with the highest breaking strength (5.7 MPa ± 0.3) while the silk-TS-4210 had the highest extension at break (215.1% ± 12.5). The films prepared from silk-TS-4210 were cytocompatible to support the adhesion and proliferation of human mesenchymal stem cells, with improvements compared to the other samples likely due to the porous morphology of these films.
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The FTIR spectrum of silk fibroin (SF) shows main characteristic bands at 1641 cm−1 (Amide I), 1514 cm−1 (Amide II), and 1234 cm−1 (Amide III), related to β-sheet formation.
“For SF (Figure 1C), the main characteristic bands were observed at 1641 cm⁻¹, corresponding to C=O stretching (Amide I); 1514 cm⁻¹, associated with Amide II vibrations, including in-plane N-H bending and C-N stretching; and 1234 cm⁻¹, corresponding to Amide III, resulting from N-C stretching and C=O bending, related to β-sheet formation [27,36].”
Citations
Cites
Materials fabrication from Bombyx mori silk fibroin
Rockwood, D. N., Preda, R. C., Yücel, T., Wang, X., Lovett, M. L., & Kaplan, D. L. (2011) · Nature Protocols · doi:10.1038/nprot.2011.379 · Cited by 3,149
Self-citationMechanism of silk processing in insects and spiders
Jin, H., & Kaplan, D. L. (2003) · Nature · doi:10.1038/nature01809 · Cited by 1,391
Self-citationHu, X., Kaplan, D. L., & Cebe, P. (2006) · Macromolecules · doi:10.1021/ma0610109 · Cited by 1,263
Self-citationMartin, J. Y., Schwartz, Z., Hummert, T. W., Schraub, D. M., Simpson, J., Lankford, J., Dean, D. D., Cochran, D. L., & Boyan, B. D. (1995) · Journal of Biomedical Materials Research · doi:10.1002/jbm.820290314 · Cited by 1,113
Bone formation by three-dimensional stromal osteoblast culture in biodegradable polymer scaffolds
Ishaug, S. L., Crane, G. M., Miller, M. J., Yasko, A. W., Yaszemski, M. J., & Mikos, A. G. (1997) · Journal of Biomedical Materials Research · doi:10.1002/(sici)1097-4636(199707)36:1 · Cited by 832
In vitro degradation of silk fibroin
Horan, R. L., Antle, K. A., Collette, A. L., Wang, Y., Huang, J., Moreau, J. E., Volloch, V., Kaplan, D. L., & Altman, G. H. (2004) · Biomaterials · doi:10.1016/j.biomaterials.2004.09.020 · Cited by 741
Self-citationSonication-induced gelation of silk fibroin for cell encapsulation
Wang, X., Kluge, J. A., Leisk, G. G., & Kaplan, D. L. (2007) · Biomaterials · doi:10.1016/j.biomaterials.2007.11.003 · Cited by 687
Self-citationPractical considerations in refolding proteins from inclusion bodies
Tsumoto, K., Ejima, D., Kumagai, I., & Arakawa, T. (2003) · Protein Expression and Purification · doi:10.1016/s1046-5928(02)00641-1 · Cited by 452
Structural characteristics and properties of the regenerated silk fibroin prepared from formic acid
Um, I. C., Kweon, H., Park, Y. H., & Hudson, S. M. (2001) · International Journal of Biological Macromolecules · doi:10.1016/s0141-8130(01)00159-3 · Cited by 436
Silk nanospheres and microspheres from silk/pva blend films for drug delivery
Wang, X., Yücel, T., Lü, Q., Hu, X., & Kaplan, D. L. (2009) · Biomaterials · doi:10.1016/j.biomaterials.2009.11.002 · Cited by 435
Self-citationSilk-based biomaterials for sustained drug delivery
Yücel, T., Lovett, M. L., & Kaplan, D. L. (2014) · Journal of Controlled Release · doi:10.1016/j.jconrel.2014.05.059 · Cited by 360
Self-citationProduction of spider silk proteins in tobacco and potato
Scheller, J., Gührs, K., Große, F., & Conrad, U. (2001) · Nature Biotechnology · doi:10.1038/89335 · Cited by 354
Effect of Processing on Silk-Based Biomaterials: Reproducibility and Biocompatibility
Wray, L. S., Hu, X., Gallego, J., Georgakoudi, I., Omenetto, F., Schmidt, D. F., & Kaplan, D. (2011) · Journal of Biomedical Materials Research. Part B - Applied biomaterials · doi:10.1002/jbm.b.31875 · Cited by 336
Self-citationPreparation of undegraded native molecular fibroin solution from silkworm cocoons
Yamada, H., Nakao, H., Takasu, Y., et al. (2001) · Materials Science and Engineering C · doi:10.1016/s0928-4931(01)00207-7 · Cited by 315
Chen, X., Shao, Z., Marinković, N., Miller, L. M., Zhou, P., & Chance, M. R. (2001) · Biophysical Chemistry · doi:10.1016/s0301-4622(00)00213-1 · Cited by 296
Silk sericin and its applications: A review
Padamwar, M. N., & Pawar, A. (2004) · Journal of Scientific & Industrial Research · Cited by 231
Insoluble and Flexible Silk Films Containing Glycerol
Lu, S., Wang, X., Lü, Q., Zhang, X., Kluge, J. A., Uppal, N., Omenetto, F. G., & Kaplan, D. L. (2009) · Biomacromolecules · doi:10.1021/bm900993n · Cited by 220
Self-citationPrimary structure of the silk fibroin light chain determined by cDNA sequencing and peptide analysis
Yamaguchi, K., Kikuchi, Y., Takagi, T., Kikuchi, A., Oyama, F., SHIMURA, K., & Mizuno, S. (1989) · Journal of Molecular Biology · doi:10.1016/0022-2836(89)90295-7 · Cited by 206
Effect of regeneration of liquid silk fibroin on its structure and characterization
Wang, H.-Y., & Zhang, Y. (2012) · Soft Matter · doi:10.1039/c2sm26945g · Cited by 187
Preparation and characterization of silk fibroin as a biomaterial with potential for drug delivery
Zhang, H., Li, L., Dai, F., et al. (2012) · Journal of Translational Medicine · doi:10.1186/1479-5876-10-117 · Cited by 174
The role of formic acid in solution stability and crystallization of silk protein polymer
Um, I. C., Kweon, H., Lee, K. G., et al. (2003) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2003.08.004 · Cited by 170
Effect of Various Dissolution Systems on the Molecular Weight of Regenerated Silk Fibroin
Wang, Q. L., Chen, Q., Yang, Y., et al. (2012) · Biomacromolecules · doi:10.1021/bm301741q · Cited by 149
Silk dissolution and regeneration at the nanofibril scale
Zhang, F., Lü, Q., Ming, J., et al. (2014) · Journal of Materials Chemistry B · doi:10.1039/c3tb21582b · Cited by 135
Optical rotatory dispersion and circular dichroism of the beta-form of silk fibroin in solution.
Iizuka, E., & Yang, J. (1966) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.55.5.1175 · Cited by 127
Dubey, P., Murab, S., Karmakar, S., Chowdhury, P., & Ghosh, S. (2015) · Biomacromolecules · doi:10.1021/acs.biomac.5b01258 · Cited by 100
Ko, J. S., Yoon, K., Ki, C. S., Kim, H. J., Bae, D. G., Lee, K. H., Park, Y. H., & Um, I. C. (2013) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2012.12.041 · Cited by 74
Pritchard, E. M., Valentin, T., Boison, D., & Kaplan, D. L. (2010) · Biomaterials · doi:10.1016/j.biomaterials.2010.09.055 · Cited by 63
Self-citationChung, D. E., & Um, I. C. (2014) · Fibers and Polymers · doi:10.1007/s12221-014-0153-8 · Cited by 49
Silk : processing, properties and applications
Babu, K. M. (2013) · Medical Entomology and Zoology · Cited by 48
Mechanical behavior comparison of spider and silkworm silks using molecular dynamics at atomic scale
Lee, M., Kwon, J., & Na, S. (2016) · Physical Chemistry Chemical Physics · doi:10.1039/c5cp06809f · Cited by 36
Silk scaffolds for dental tissue engineering
Jindal, S. K., Kiamehr, M., Sun, W., & Yang, X. (2014) · Elsevier eBooks · doi:10.1533/9780857097064.3.403 · Cited by 35
Babu, K. M. (2013) · Woodhead Publishing Limited eBooks · doi:10.1533/9781782421580 · Cited by 25
Deshpande, S. S., & Damodaran, S. (1991) · Journal of Protein Chemistry · doi:10.1007/bf01024660 · Cited by 19
Flagged first, then by citations
Research works printed but not linked: 3
- Kundu. Silk biomaterials for tissue engineering and regenerative medicine foreword, Cambridge: Woodhead Publishing, 2014, pp. 78–99.
- Padamwar MN, 2004, J Sci Ind Res, 63, 323
- Ajisawa A, 1998, J Seric Sci, 67, 91
Cited by
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Silk fibroin as a functional biomaterial for tissue engineering
Sun, W., Gregory, D. A., Tomeh, M. A., & Zhao, X. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22031499 · Cited by 552
Antunes, B. S. L., Pedrini, F., Komatsu, D., Asami, J., Dicko, C., & Duek, E. A. R. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.154129
Metadata
- Authors
- Zheng, Z., Guo, S., Liu, Y., Wu, J., Li, G., Liu, M., Wang, X., & Kaplan, D.
- Affiliations
- Soochow University (CN)
- Tufts University (US)
- Corresponding author
- Wang, Xiaoqin
- Venue
- Journal of Biomaterials Applications
- Publisher
- SAGE Publications
- Published
- 2016-07-09
- Volume
- 31
- Issue
- 3
- Pages
- 450-463
- ISSN
- 0885-3282 (ISSN-L)
- 1530-8022
- OpenAlex
- W2417640789
- Cited by
- 45
- References
- 33
- Citations by year
- 2026: 4 · 2025: 4 · 2024: 4 · 2023: 10 · 2022: 4 · 2021: 11 · 2020: 3 · 2019: 1 · 2018: 3 · 2017: 1
- FWCI
- 0.68
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Biomaterials Applications (publishedVersion)
- PubMed (publishedVersion)
- 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 › Biomaterials › Electrospun Nanofibers in Biomedical Applications
- Keywords
- silk fibroin, Bombyx mori, protein purification, dialysis, β-sheet content, protein aggregation, silk films, mechanical properties, cytocompatibility, mesenchymal stem cells, porous films
- MeSH terms
- Animals, Biocompatible Materials, Bromides, Cell Adhesion, Cells, Cultured, Fibroins, Humans, Indicators and Reagents, Materials Testing, Bombyx, Urea, Lithium Compounds, Silk, Cell Proliferation, Mesenchymal Stem Cells
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