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A simple process for dry spinning of regenerated silk fibroin aqueous solution

Published online by Cambridge University Press:  11 October 2013

Yuan Jin
Affiliation:
State Key Laboratory for Modification of Chemical Fibers and Polymer Materials, College of Materials Science and Engineering, Donghua University, Shanghai 201620, People’s Republic of China
Yaopeng Zhang
Affiliation:
State Key Laboratory for Modification of Chemical Fibers and Polymer Materials, College of Materials Science and Engineering, Donghua University, Shanghai 201620, People’s Republic of China
Yichun Hang
Affiliation:
State Key Laboratory for Modification of Chemical Fibers and Polymer Materials, College of Materials Science and Engineering, Donghua University, Shanghai 201620, People’s Republic of China
Huili Shao*
Affiliation:
State Key Laboratory for Modification of Chemical Fibers and Polymer Materials, College of Materials Science and Engineering, Donghua University, Shanghai 201620, People’s Republic of China
Xuechao Hu*
Affiliation:
State Key Laboratory for Modification of Chemical Fibers and Polymer Materials, College of Materials Science and Engineering, Donghua University, Shanghai 201620, People’s Republic of China
*
a)Address all correspondence to this author. e-mail: hlshao@dhu.edu.cn
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Abstract

The conventional process for preparing dry spinnable regenerated silk fibroin (RSF) aqueous solution needs not only an addition of Ca2+ but also an adjustment of pH value. In this work, an RSF dry spinning dope was prepared by using a simplified method with solely adding Ca2+. Compared with the conventional RSF solution, the simply prepared aqueous solution showed similar content of β-sheet conformation and diameter of RSF aggregates but lower viscosity. Furthermore, the posttreated RSF fiber dry-spun from this simply prepared solution showed higher crystallinity and crystalline orientation, smaller crystallite size, and better mechanical properties. It could be concluded that Ca2+ played a much more important role than pH value in improving the structures and properties of RSF spinning solution and fibers. Therefore, the step of adjusting pH value could be excluded in the process of preparing high performance RSF fibers.

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Articles
Copyright
Copyright © Materials Research Society 2013 

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References

REFERENCES

Shao, Z.Z. and Vollrath, F.: Surprising strength of silkworm silk. Nature 418, 741 (2002).CrossRefGoogle ScholarPubMed
Vepari, C. and Kaplan, D.L.: Silk as a biomaterial. Prog. Polym. Sci. 32, 991 (2007).CrossRefGoogle Scholar
Kanekatsu, R.: New regenerated fibers composed of silk fibroins and cellulose. Sen-I Gakkaishi 60, 21 (2004).CrossRefGoogle Scholar
Zhou, G.Q., Chen, X., and Shao, Z.Z.: The artificial spinning based on silk proteins. Prog. Chem. 18, 933 (2006).Google Scholar
Kawahara, Y., Nakayama, A., Matsumura, N., Yoshioka, T., and Tsuji, M.: Structure for electro-spun silk fibroin nanofibers. J. Appl. Polym. Sci. 107, 3681 (2008).CrossRefGoogle Scholar
Matsumoto, K., Uejima, H., Iwasaki, T., Sano, Y., and Sumino, H.J.: Studies on regenerated protein fibers. 3. Production of regenerated silk fibroin fiber by the self-dialyzing wet spinning method. J. Appl. Polym. Sci. 60, 503 (1996).3.0.CO;2-S>CrossRefGoogle Scholar
Um, I.C., Kweon, H.Y., Lee, K.G., Ihm, D.W., Lee, J.H., and Park, Y.H.: Wet spinning of silk polymer—I. Effect of coagulation conditions on the morphological feature of filament. Int. J. Biol. Macromol. 34, 89 (2004).CrossRefGoogle ScholarPubMed
Um, I.C., Kweon, H.Y., Lee, K.G., Ihm, D.W., Lee, J.H., and Park, Y.H.: Wet spinning of silk polymer—II. Effect of drawing on the structural characteristics and properties of filament. Int. J. Biol. Macromol. 34, 107 (2004).CrossRefGoogle ScholarPubMed
Zhou, G.Q., Shao, Z.Z., Knight, D.P., Yan, J.P., and Chen, X.: Silk fibers extruded artificially from aqueous solutions of regenerated Bombyx mori silk fibroin are tougher than their natural counterparts. Adv. Mater. 20, 1 (2008).Google Scholar
Zhu, J.X., Zhang, Y.P., Shao, H.L., and Hu, X.C.: Electrospinning and rheology of regenerated Bombyx mori silk fibroin aqueous solutions: The effects of pH and concentration. Polymer 49, 2880 (2008).CrossRefGoogle Scholar
Wei, W., Zhang, Y.P., Shao, H.L., and Hu, X.C.: Posttreatment of the dry-spun fibers obtained from regenerated silk fibroin aqueous solution in ethanol aqueous solution. J. Mater. Res. 26, 1100 (2011).CrossRefGoogle Scholar
Wei, W., Zhang, Y.P., Zhao, Y.M., Shao, H.L., and Hu, X.C.: Studies on the post-treatment of the dry-spun fibers from regenerated silk fibroin solution: Post-treatment agent and method. Mater. Des. 36, 816 (2012).CrossRefGoogle Scholar
Wei, W., Zhang, Y.P., Zhao, Y.M., Shao, H.L., and Hu, X.C.: Bio-inspired capillary dry spinning of regenerated silk fibroin aqueous solution. Mater. Sci. Eng., C 31, 1602 (2011).CrossRefGoogle Scholar
Sun, M.J., Zhang, Y.P., Zhao, Y.M., Luo, J., Shao, H.L., and Hu, X.C.: The structure–property relationships of artificial silk fabricated by dry-spinning process. J. Mater. Chem. 22, 18372 (2012).CrossRefGoogle Scholar
Zhou, L., Chen, X., Shao, Z.Z., Huang, Y.F., and Knight, D.P.: Effect of metallic ions on silk formation the mulberry silkworm, Bombyx mori. J. Phys. Chem. B 109, 16937 (2005).CrossRefGoogle ScholarPubMed
Glisovic, A. and Salditt, T.J.: Temperature dependent structure of spider silk by X-ray diffraction. Appl. Phys. A 87, 63 (2007).CrossRefGoogle Scholar
Shen, Y., Johnson, M.A., and Martin, D.C.: Microstructural characterization of Bombyx mori silk fibers. Macromolecules 31, 8857 (1998).CrossRefGoogle Scholar
Foo, C.W.P., Bini, E., Hensman, J., Knight, D.P., Lewis, R.V., and Kaplan, D.L.: Role of pH and charge on silk protein assembly in insects and spiders. Appl. Phys. A 82, 223 (2006).CrossRefGoogle Scholar
Shao, J.Z., Zheng, J.H., Liu, J.Q., and Carr, C.M.: Fourier transform Raman and Fourier transform infrared spectroscopy studies of silk fibroin. J. Appl. Polym. Sci. 96, 1999 (2005).CrossRefGoogle Scholar
Monti, P., Freddi, G., Bertoluzza, A., Kasai, N., and Tsukada, M.: Raman spectroscopic studies of silk fibroin from Bombyx mori. J. Raman Spectrosc. 29, 297 (1998).3.0.CO;2-G>CrossRefGoogle Scholar
Zhou, P., Xie, X., Deng, F., Ping, Z., Xun, X., and Feng, D.: Effects of pH and calcium ions on the conformational transitions in silk fibroin using 2D Raman correlation spectroscopy and C-13 solid-state NMR. Biochemistry 43, 11302 (2004).CrossRefGoogle Scholar
Nagano, A., Sato, H., Tanioka, Y., Nakazawa, Y., Knight, D., and Asakura, T.: Characterization of a Ca binding-amphipathic silk-like protein and peptide with the sequence (Glu)(8)(Ala-Gly-Ser-Gly-Ala-Gly)(4) with potential for bone repair. Soft Matter 8, 741 (2012).CrossRefGoogle Scholar