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Posttreatment of the dry-spun fibers obtained from regenerated silk fibroin aqueous solution in ethanol aqueous solution

Published online by Cambridge University Press:  19 April 2011

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

Regenerated silk fibroin (RSF) fibers were directly dry-spun from RSF aqueous solutions into air. To improve mechanical properties of fiber, the as-spun fibers were postdrawn in 80 vol.% ethanol aqueous solution, in which an immersion process was performed subsequently. With the increase in draw ratio, the fibers show substantial improvements of orientation and mechanical properties. Quantitative analysis of Fourier transform infrared spectroscopy indicates that the ratio of β-sheet to α-helix conformation increases sharply at the beginning of immersion process, then approaches a constant value after 90 min of immersion. All fibers exhibit very smooth surfaces. There is no obvious relationship between the pH of the spinning dope and the mechanical properties of the regenerated fibers. The breaking stress of the posttreated fiber is improved up to 301 MPa, which approaches that of degummed silk. The posttreated fiber is over three times the breaking energy of degummed silk.

Keywords

PolymerFiberBiomimetic (assembly)
Type
Articles
Information
Journal of Materials Research , Volume 26 , Issue 9 , 14 May 2011 , pp. 1100 - 1106
Copyright
Copyright © Materials Research Society 2011

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References

REFERENCES

1.Gosline, J.M., Demont, M.E., and Denny, M.W.: The structure and properties of spider silk. Endeavour 10, 37 (1986).CrossRefGoogle Scholar
2.Tirrell, D.A.: Putting a new spin on spider silk. Science 271, 39 (1996).Google Scholar
3.Shao, Z.Z. and Vollrath, F.: Materials: Surprising strength of silkworm silk. Nature 418, 741 (2002).Google Scholar
4.Huang, M.R. and Li, X.G.: Comparison and review of high performance fibers. J. Textile Res. (Chinese). 18, 62 (1997).Google Scholar
5.Li, X.G., Huang, M.R., and Hua, Y.M.: Structure and properties of liquid crystalline cellulose and its derivatives materials. J. Tongji Univ. 30, 464 (2002).Google Scholar
6.Vollrath, F. and Knight, D.P.: Liquid crystalline spinning of spider silk. Nature 410, 541 (2001).CrossRefGoogle ScholarPubMed
7.Jin, H.J. and Kaplan, D.L.: Mechanism of silk processing in insects and spiders. Nature 424, 1057 (2003).CrossRefGoogle ScholarPubMed
8.Viney, C.: Natural silks: Archetypal supramolecular assembly of polymer fibres. Supramol. Sci. 4, 75 (1997).CrossRefGoogle Scholar
9.Wilding, M.A. and Hearle, J.W.S.: Polymeric Materials Encyclopedia, 1st ed. (CRC press, Boca Raton, FL, USA, 1996). pp. 8307, 8322.Google Scholar
10.Vendrely, C. and Scheibel, T.: Biotechnological production of spider-silk proteins enables new applications. Macromol. Biosci. 7, 401 (2007).CrossRefGoogle ScholarPubMed
11.Metwalli, E., Slotta, U., Darko, C., Roth, S.V., Scheibel, T., and Papadakis, C.M.: Structural changes of thin films from recombinant spider silk proteins upon post-treatment. Appl. Phys. A Mater. 89, 655 (2007).CrossRefGoogle Scholar
12.Anderson, J.P.: Morphology and crystal structure of a recombinant silk-like molecule, SLP4. Biopolymers 45, 307 (1998).3.0.CO;2-P>CrossRefGoogle Scholar
13.Heslot, H.: Artificial fibrous proteins: A review. Biochimie 80, 19 (1998).CrossRefGoogle ScholarPubMed
14.Ishizaka, H., Watanabe, Y., Ishida, K., and Fukumoto, O.: Regenerated silk prepared from ortho phosphoric acid solution of fibroin. Nippon Sanshigaku Zasshi. 58, 87 (1989).Google Scholar
15.Yao, J.M., Masuda, H., Zhao, C.H., and Asakura, T.: Artificial spinning and characterization of silk fiber from Bombyx mori silk fibroin in hexafluoroacetone hydrate. Macromolecules 35, 6 (2002).CrossRefGoogle Scholar
16.Ha, S.W., Park, Y.H., and Hudson, S.M.: Dissolution of Bombyx mori silk fibroin in the calcium nitrate tetrahydrate-methanol system and aspects of wet spinning of fibroin solution. Biomacromolecules 4, 488 (2003).CrossRefGoogle ScholarPubMed
17.Ha, S.W., Tonelli, A.E., and Hudson, S.M.: Structural studies of Bombyx mori silk fibroin during regeneration from solutions and wet fiber spinning. Biomacromolecules 6, 1722 (2005).CrossRefGoogle ScholarPubMed
18.Um, I.C., Ki, C.S., Lee, K.H., Baek, D.H., Hattori, M., Ihm, D.W., and Park, Y.H.: Dissolution and wet spinning of silk fibroin using phosphoric acid/formic acid mixture solvent system. J. Appl. Polym. Sci. 105, 1605 (2007).Google Scholar
19.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. (Deerfield Beach Fla.) 21, 366 (2009).CrossRefGoogle Scholar
20.Wei, W., Zhang, Y.P., Zhao, Y.M., Shao, H.L., and Hu, X.C.: Dry spinning of regenerated silk fibroin aqueous solution. J. Funct. Polym. (Chinese) 22, 229 (2009).Google Scholar
21.Wei, W., Zhang, Y.P., Zhao, Y.M., Shao, H.L., and Hu, X.C.: Post-treatment agent and method of dry-spun fibers from regenerated silk fibroin solution. J. Funct. Polym. (Chinese) 23, 230 (2010).Google Scholar
22.Fossey, S.A. and Kaplan, D.L.: Polymer Data Handbook, 1st ed. (Oxford University Press, New York, 1999), pp. 970, 974.Google Scholar
23.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
24.Bhat, N.V. and Ahirrao, S.M.: Investigation of the structure of silk film regenerated with lithium thiocyanate solution. J. Polym. Sci. A-1: Polym. Chem. 21, 1273 (1983).Google Scholar
25.Mathur, A.B., Tonelli, A., Rathke, T., and Hudson, S.: The dissolution and characterization of Bombyx mori silk fibroin in calcium nitrate methanol solution and the regeneration of films. Biopolymers 42, 61 (1997).3.0.CO;2-#>CrossRefGoogle Scholar
26.Khan, M.M.I.R., Morikawa, H., Gotoh, Y., Miura, M., Ming, Z., Sato, Y., and Iwasa, M.: Structural characteristics and properties of Bombyx mori silk fiber obtained by different artificial forcibly silking speeds. Int. J. Biol. Macromol. 42, 264 (2008).CrossRefGoogle ScholarPubMed
27.Um, I.C., Ki, C.S., Kweon, H.Y., Lee, K.G., Ihm, D.W., 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
28.Chen, X., Shao, Z., Marinkovic, N.S., Miller, L.M., Zhou, P., and Chance, M.R.: Conformation transition kinetics of regenerated Bombyx mori silk fibroin membrane monitored by time-resolved FTIR spectroscopy. Biophys. Chem. 89, 25 (2001).CrossRefGoogle ScholarPubMed
29.Chen, X., Knight, D.P., Shao, Z.Z., and Vollrath, F.: Conformation transition in silk protein films monitored by time-resolved fourier transform infrared spectroscopy: Effect of potassium ions on Nephila spidroin films. Biochemistry (Moscow) 41, 14944 (2002).CrossRefGoogle ScholarPubMed
30.Chen, X., Shao, Z.Z., Knight, D.P., and Vollrath, F.: Conformation transition kinetics of Bombyx mori silk protein. Proteins 68, 223 (2007).CrossRefGoogle ScholarPubMed
31.Hu, X., Kaplan, D., and Cebe, P.: Effect of water on the thermal properties of silk fibroin. Thermochim. Acta 461, 137 (2007).CrossRefGoogle Scholar
32.Drummy, L.F., Phillips, D.M., Stone, M.O., Farmer, B.L., and Naik, R.R.: Thermally induced alpha-helix to beta-sheet transition in regenerated silk fibers and films. Biomacromolecules 6, 3328 (2005).Google Scholar