Water-insoluble silk films with silk I structure
Open accessAbstract
Water-insoluble regenerated silk materials are normally produced by increasing the beta-sheet content (silk II). In the present study water-insoluble silk films were prepared by controlling the very slow drying of Bombyx mori silk solutions, resulting in the formation of stable films with a predominant silk I instead of silk II structure. Wide angle X-ray scattering indicated that the silk films stabilized by slow drying were mainly composed of silk I rather than silk II, while water- and methanol-annealed silk films had a higher silk II content. The silk films prepared by slow drying had a globule-like structure at the core surrounded by nano-filaments. The core region was composed of silk I and silk II, surrounded by hydrophilic nano-filaments containing random turns and alpha-helix secondary structures. The insoluble silk films prepared by slow drying had unique thermal, mechanical and degradative properties. Differential scanning calorimetry results revealed that silk I crystals had stable thermal properties up to 250 degrees C, without crystallization above the T(g), but degraded at lower temperatures than silk II structure. Compared with water- and methanol-annealed films the films prepared by slow drying had better mechanical ductility and were more rapidly enzymatically degraded, reflecting the differences in secondary structure achieved via differences in post processing of the cast silk films. Importantly, the silk I structure, a key intermediate secondary structure for the formation of mechanically robust natural silk fibers, was successfully generated by the present approach of very slow drying, mimicking the natural process. The results also point to a new mode of generating new types of silk biomaterials with enhanced mechanical properties and increased degradation rates, while maintaining water insolubility, along with a low beta-sheet content.
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An exothermic transition in SFMA centered at ~224.0 °C is associated with thermally induced structural reorganization and secondary β-sheet formation within the fibroin matrix.
“Importantly, an exothermic transition centered at ~ 224.0 °C was detected and is associated with thermally induced structural reorganization and secondary β-sheet formation within the fibroin matrix, as described by Freddi et al., 1999 andLu et al., 2010 [49,50].”
From Montmorillonite-reinforced methacrylated collagen/methacrylated silk fibroin hydrogel-based inks: rheological and physicochemical characterization for bone scaffold applications (2026) · cites this paper as [50]
Section 3.2 (Thermal stability; page not provided) links a crystallization peak in soluble silk fibroin films at about 213 °C to conversion of non-crystalline structures into β-sheets. This supports the proposed interpretation of a thermal transition, but the paper does not report an SFMA transition centered at about 224 °C. (LLM, conf=0.85)
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Cites
Vepari, C., & Kaplan, D. L. (2007) · Progress in Polymer Science · doi:10.1016/j.progpolymsci.2007.05.013 · Cited by 2,579 · see citing works
Self-citationMechanism of silk processing in insects and spiders
Jin, H., & Kaplan, D. L. (2003) · Nature · doi:10.1038/nature01809 · Cited by 1,379 · see citing works
Self-citationHu, X., Kaplan, D. L., & Cebe, P. (2006) · Macromolecules · doi:10.1021/ma0610109 · Cited by 1,251 · see citing works
Self-citationThree-dimensional aqueous-derived biomaterial scaffolds from silk fibroin
Kim, U., Park, J. H., Kim, H. J., Wada, M., & Kaplan, D. L. (2004) · Biomaterials · doi:10.1016/j.biomaterials.2004.07.044 · Cited by 979 · see citing works
Self-citationStructure and Properties of Silk Hydrogels
Kim, U.-J., Park, J. H., Li, C., Jin, H., Valluzzi, R., & Kaplan, D. L. (2004) · Biomacromolecules · doi:10.1021/bm0345460 · Cited by 857 · see citing works
Self-citationIn vivo degradation of three-dimensional silk fibroin scaffolds
Wang, Y., Rudym, D., Walsh, A., Abrahamsen, L., Kim, H.-J., Kim, H. S., Kirker‐Head, C. A., & Kaplan, D. L. (2008) · Biomaterials · doi:10.1016/j.biomaterials.2008.05.002 · Cited by 788 · see citing works
Self-citationElectrospinning Bombyx mori Silk with Poly(ethylene oxide)
Jin, H., Fridrikh, S. V., Rutledge, G. C., & Kaplan, D. L. (2002) · Biomacromolecules · doi:10.1021/bm025581u · Cited by 715 · see citing works
Self-citationWater‐Stable Silk Films with Reduced β‐Sheet Content
Jin, H., Park, J., Karageorgiou, V., Kim, U.-J., Valluzzi, R., Cebe, P., & Kaplan, D. L. (2005) · Advanced Functional Materials · doi:10.1002/adfm.200400405 · Cited by 610 · see citing works
Self-citationStructural 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 · see citing works
Mechanical Properties of Robust Ultrathin Silk Fibroin Films
Jiang, C., Wang, X., Gunawidjaja, R., Lin, Y. ‐., Gupta, M. K., Kaplan, D. L., Naik, R. R., & Tsukruk, V. V. (2007) · Advanced Functional Materials · doi:10.1002/adfm.200601136 · Cited by 404 · see citing works
Self-citationDynamic protein–water relationships during β-sheet formation
Hu, X., Kaplan, D., & Cebe, P. (2008) · Macromolecules · doi:10.1021/ma071551d · Cited by 315 · see citing works
Self-citationMechanical Properties of Electrospun Silk Fibers
Wang, M., Jin, H., Kaplan, D. L., & Rutledge, G. C. (2004) · Macromolecules · doi:10.1021/ma048988v · Cited by 314 · see citing works
Self-citationSilk microspheres for encapsulation and controlled release
Wang, X., Wenk, E., Matsumoto, A., Meinel, L., Li, C. C., & Kaplan, D. L. (2006) · Journal of Controlled Release · doi:10.1016/j.jconrel.2006.11.021 · Cited by 293 · see citing works
Self-citationConformational Transitions in Model Silk Peptides
Wilson, D. L., Valluzzi, R., & Kaplan, D. L. (2000) · Biophysical Journal · doi:10.1016/s0006-3495(00)76813-5 · Cited by 253 · see citing works
Self-citationBiomaterial Films of Bombyx Mori Silk Fibroin with Poly(ethylene oxide)
Jin, H., Park, J. H., Valluzzi, R., Cebe, P., & Kaplan, D. L. (2004) · Biomacromolecules · doi:10.1021/bm0343287 · Cited by 238 · see citing works
Self-citationLiu, H., Fan, H., Wang, Y., Toh, S. L., & Goh, J. C. (2007) · Biomaterials · doi:10.1016/j.biomaterials.2007.10.035 · Cited by 210 · see citing works
Porous silk fibroin 3‐D scaffolds for delivery of bone morphogenetic protein‐2 in vitro and in vivo
Karageorgiou, V., Tomkins, M., Fajardo, R., Meinel, L., Snyder, B. D., Wade, K., Chen, J., Vunjak‐Novakovic, G., & Kaplan, D. L. (2006) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.30728 · Cited by 210 · see citing works
Self-citationTerry, A. E., Knight, D. P., Porter, D., et al. (2004) · Biomacromolecules · doi:10.1021/bm034381v · Cited by 200 · see citing works
The preparation of regenerated silk fibroin microspheres
Cao, Z., Chen, X., Yao, J., et al. (2007) · Soft Matter · doi:10.1039/b703139d · Cited by 190 · see citing works
Effect of Metallic Ions on Silk Formation in the Mulberry Silkworm, Bombyx m ori
Li, Z., Chen, X., Shao, Z., Huang, Y., & Knight, D. P. (2005) · The Journal of Physical Chemistry B · doi:10.1021/jp050883m · Cited by 183 · see citing works
Demura, M., & Asakura, T. (1989) · Biotechnology and Bioengineering · doi:10.1002/bit.260330513 · Cited by 132 · see citing works
Preparation of non-woven mats from all-aqueous silk fibroin solution with electrospinning method
Chen, C., Cao, C., Ma, X., et al. (2006) · Polymer · doi:10.1016/j.polymer.2006.07.009 · Cited by 129 · see citing works
Transition to a β-Sheet-Rich Structure in Spidroin in Vitro: The Effects of pH and Cations
Dicko, C., Kenney, J. M., Knight, D. P., et al. (2004) · Biochemistry · doi:10.1021/bi0483413 · Cited by 113 · see citing works
Lv, Q., Hu, K., Feng, Q., & Cui, F. (2007) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.31366 · Cited by 111 · see citing works
Demura, M., Asakura, T., & Kuroo, T. (1989) · Biosensors · doi:10.1016/0265-928x(89)80002-1 · Cited by 103 · see citing works
Cytocompatibility and blood compatibility of multifunctional fibroin/collagen/heparin scaffolds
Lü, Q., Zhang, S., Hu, K., et al. (2007) · Biomaterials · doi:10.1016/j.biomaterials.2007.01.031 · Cited by 101 · see citing works
An Unstable Lattice in Silk Fibroin
Kratky, O., Schauenstein, E., & Sekora, A. (1950) · Nature · doi:10.1038/165319a0 · Cited by 71 · see citing works
Phase Behavior and Hydration of Silk Fibroin
Sohn, S., Strey, H. H., & Gido, S. P. (2004) · Biomacromolecules · doi:10.1021/bm0343693 · Cited by 62 · see citing works
Pyda, M., Hu, X., & Cebe, P. (2008) · Macromolecules · doi:10.1021/ma8003357 · Cited by 47 · see citing works
Self-citationHan, J., & Herzfeld, J. (1998) · Biopolymers · doi:10.1002/(sici)1097-0282(19980405)45:4 · Cited by 12 · see citing works
Structure and physical properties of silk fibroin/polyacrylamide blend films
Freddi, G., Tsukada, M., & Beretta, S. (1999) · Journal of Applied Polymer Science · doi:10.1002/(sici)1097-4628(19990307)71:10
Flagged first, then by citations
Cited by
Sorted by citations
Dissolvable films of silk fibroin for ultrathin conformal bio-integrated electronics
Kim, D.-H., Viventi, J., Amsden, J. J., Xiao, J., Vigeland, L., Kim, Y.-S., Blanco, J. A., Panilaitis, B., Frechette, E. S., Contreras, D., et al. (2010) · Nature Materials · doi:10.1038/nmat2745 · Cited by 1,721 · see citing works
Self-citationSilk fibroin biomaterials for tissue regenerations
Kundu, B., Rajkhowa, R., Kundu, S. C., & Wang, X. (2013) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2012.09.043 · Cited by 1,391 · see citing works
Self-citationSilk 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 · see citing works
Degradation mechanism and control of silk fibroin
Lu, Q., Zhang, B., Li, M., Zuo, B., Kaplan, D. L., Huang, Y., & Zhu, H. (2011) · Biomacromolecules · doi:10.1021/bm101422j · Cited by 344 · see citing works
Self-citationSilk scaffolds in bone tissue engineering: An overview
Bhattacharjee, P., Kundu, B., Naskar, D., Kim, H.-W., Maiti, T. K., Bhattacharya, D., & Kundu, S. C. (2017) · Acta Biomaterialia · doi:10.1016/j.actbio.2017.09.027 · Cited by 318 · see citing works
Tien, L. W., Wu, F., Tang‐Schomer, M. D., Yoon, E., Omenetto, F. G., & Kaplan, D. L. (2013) · Advanced Functional Materials · doi:10.1002/adfm.201203716 · Cited by 136 · see citing works
Self-citationChemical, thermal, time, and enzymatic stability of silk materials with silk I structure
Zhao, M., Qi, Z., Tao, X., Newkirk, C., Hu, X., & Lu, S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22084136 · Cited by 130 · see citing works
Self-citationMa, Y., Wang, H., Wang, Q., Cao, X., & Gao, H. (2023) · Chemical Engineering Journal · doi:10.1016/j.cej.2022.139424 · Cited by 103 · see citing works
Tan, X. H., Liu, L., Mitryashkin, A., Wang, Y., & Goh, J. C. H. (2022) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.2c00313 · Cited by 36 · see citing works
Stretchable silk fibroin hydrogels
Oral, C. B., Yetiskin, B., & Okay, O. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.08.040 · Cited by 35 · see citing works
Zadegan, S., Nourmohammadi, J., Vahidi, B., & Haghighipour, N. (2019) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2019.04.165 · Cited by 31 · see citing works
Li, W., Shi, X., Zhang, D., Hu, J., Zhao, S., Ye, S., Wang, J., Liu, X., Zhang, Q., Wang, Z., et al. (2025) · Journal of Materials Chemistry B · doi:10.1039/d5tb00275c · Cited by 5 · see citing works
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
- Authors
- Lu, Q., Hu, X., Wang, X., Kluge, J. A., Lu, S., Cebe, P., & Kaplan, D. L.
- Affiliations
- Tufts University (US)
- Corresponding author
- Kaplan, David L.
- Venue
- Acta Biomaterialia
- Publisher
- Elsevier BV
- Published
- 2010-04
- Volume
- 6
- Issue
- 4
- Pages
- 1380-1387
- ISSN
- 1742-7061 (ISSN-L)
- PMC
- PMC2830340
- OpenAlex
- W2017686654
- Cited by
- 654
- References
- 31
- Citations by year
- 2026: 32 · 2025: 32 · 2024: 42 · 2023: 38 · 2022: 46 · 2021: 59 · 2020: 71 · 2019: 49 · 2018: 56 · 2017: 49 · 2016: 36 · 2015: 36 · 2014: 38 · 2013: 17 · 2012: 28
- FWCI
- 7.61
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Acta Biomaterialia (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Science Foundation
- National Institutes of Health
- National Eye Institute (R01EY020856)
- National Institute of Biomedical Imaging and Bioengineering (R01EB003210, P41EB002520)
- National Institute of Dental and Craniofacial Research (R01DE017207)
- Air Force Office of Scientific Research
- 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 › biodegradable polymer synthesis and properties
- Keywords
- Bombyx mori silk, slow drying, β-sheet content, thermal stability, mechanical properties, enzymatic degradation, silk biomaterials
- MeSH terms
- Calorimetry, Differential Scanning, Pronase, Scattering, Radiation, Solubility, Temperature, Thermogravimetry, Time Factors, Water, X-Ray Diffraction, Protein Structure, Secondary, Spectroscopy, Fourier Transform Infrared, Silk, Mechanical Phenomena
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