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Journal of Chemistry
Volume 2013, Article ID 640913, 7 pages
http://dx.doi.org/10.1155/2013/640913
Research Article

Acylation Modification of Antheraea pernyi Silk Fibroin Using Succinic Anhydride and Its Effects on Enzymatic Degradation Behavior

National Engineering Laboratory for Modern Silk, College of Textile and Clothing Engineering, Soochow University, No. 199 Ren’ai Road, Industrial Park, Suzhou, Jiangsu 215123, China

Received 18 December 2012; Revised 27 April 2013; Accepted 8 May 2013

Academic Editor: Debora M. Martino

Copyright © 2013 Xiufang Li et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. N. Minoura, S. I. Aiba, M. Higuchi, Y. Gotoh, M. Tsukada, and Y. Imai, “Attachment and growth of fibroblast cells on silk fibroin,” Biochemical and Biophysical Research Communications, vol. 208, no. 2, pp. 511–516, 1995. View at Publisher · View at Google Scholar · View at Scopus
  2. C. Fu, D. Porter, X. Chen, F. Vollrath, and Z. Shao, “Understanding the mechanical properties of Antheraea pernyi Silka-From primary structure to condensed structure of the protein,” Advanced Functional Materials, vol. 21, no. 4, pp. 729–737, 2011. View at Publisher · View at Google Scholar · View at Scopus
  3. H. Kweon and Y. H. Park, “Dissolution and characterization of regenerated Antheraea pernyi silk fibroin,” Journal of Applied Polymer Science, vol. 82, no. 3, pp. 750–758, 2001. View at Publisher · View at Google Scholar · View at Scopus
  4. H. Y. Kweon and Y. H. Park, “Structural and conformational changes of regenerated Antheraea pernyi silk fibroin films treated with methanol solution,” Journal of Applied Polymer Science, vol. 73, no. 14, pp. 2887–2894, 1999. View at Google Scholar
  5. H. Y. Kweon, I. C. Um, and Y. H. Park, “Thermal behavior of regenerated Antheraea pernyi silk fibroin film treated with aqueous methanol,” Polymer, vol. 41, no. 20, pp. 7361–7367, 2000. View at Publisher · View at Google Scholar · View at Scopus
  6. U. J. Kim, J. Park, H. Joo Kim, M. Wada, and D. L. Kaplan, “Three-dimensional aqueous-derived biomaterial scaffolds from silk fibroin,” Biomaterials, vol. 26, no. 15, pp. 2775–2785, 2005. View at Publisher · View at Google Scholar · View at Scopus
  7. O. Hakimi, D. P. Knight, F. Vollrath, and P. Vadgama, “Spider and mulberry silkworm silks as compatible biomaterials,” Composites Part B, vol. 38, no. 3, pp. 324–337, 2007. View at Publisher · View at Google Scholar · View at Scopus
  8. L. S. Nair and C. T. Laurencin, “Biodegradable polymers as biomaterials,” Progress in Polymer Science, vol. 32, no. 8-9, pp. 762–798, 2007. View at Publisher · View at Google Scholar · View at Scopus
  9. Q. Lu, B. Zhang, M. Li et al., “Degradation mechanism and control of silk fibroin,” Biomacromolecules, vol. 12, no. 4, pp. 1080–1086, 2011. View at Publisher · View at Google Scholar · View at Scopus
  10. R. L. Horan, K. Antle, A. L. Collette et al., “In vitro degradation of silk fibroin,” Biomaterials, vol. 26, no. 17, pp. 3385–3393, 2005. View at Publisher · View at Google Scholar · View at Scopus
  11. P. Taddei, T. Arai, A. Boschi, P. Monti, M. Tsukada, and G. Freddi, “In vitro study of the proteolytic degradation of Antheraea pernyi silk fibroin,” Biomacromolecules, vol. 7, no. 1, pp. 259–267, 2006. View at Publisher · View at Google Scholar · View at Scopus
  12. Y. Hu, Q. Zhang, R. You, L. Wang, and M. Li, “The relationship between secondary structure and biodegradation behavior of silk fibroin scaffolds,” Advances in Materials Science and Engineering, vol. 2012, Article ID 185905, 5 pages, 2012. View at Publisher · View at Google Scholar
  13. T. Arai, G. Freddi, R. Innocenti, and M. Tsukada, “Biodegradation of Bombyx mori silk fibroin fibers and films,” Journal of Applied Polymer Science, vol. 91, no. 4, pp. 2383–2390, 2004. View at Publisher · View at Google Scholar · View at Scopus
  14. M. Li, M. Ogiso, and N. Minoura, “Enzymatic degradation behavior of porous silk fibroin sheets,” Biomaterials, vol. 24, no. 2, pp. 357–365, 2003. View at Publisher · View at Google Scholar · View at Scopus
  15. C. Zhao, X. Wu, Q. Zhang, S. Yan, and M. Li, “Enzymatic degradation of Antheraea pernyi silk fibroin 3D scaffolds and fibers,” International Journal of Biological Macromolecules, vol. 48, no. 2, pp. 249–255, 2011. View at Publisher · View at Google Scholar · View at Scopus
  16. A. Kojthung, P. Meesilpa, B. Sudatis, L. Treeratanapiboon, R. Udomsangpetch, and B. Oonkhanond, “Effects of gamma radiation on biodegradation of Bombyx mori silk fibroin,” International Biodeterioration and Biodegradation, vol. 62, no. 4, pp. 487–490, 2008. View at Publisher · View at Google Scholar · View at Scopus
  17. Z. She, B. Zhang, C. Jin, Q. Feng, and Y. Xu, “Preparation and In vitro degradation of porous three-dimensional silk fibroin/chitosan scaffold,” Polymer Degradation and Stability, vol. 93, no. 7, pp. 1316–1322, 2008. View at Publisher · View at Google Scholar · View at Scopus
  18. Y. Wang, D. D. Rudym, A. Walsh et al., “In vivo degradation of three-dimensional silk fibroin scaffolds,” Biomaterials, vol. 29, no. 24-25, pp. 3415–3428, 2008. View at Publisher · View at Google Scholar · View at Scopus
  19. Y. Xu, Y. Wang, Y. Jiao, C. Zhang, and M. Li, “Enzymatic degradation properties of silk fibroin film,” Journal of Fiber Bioengineering and Informatics, vol. 4, no. 1, pp. 35–41, 2011. View at Google Scholar
  20. S. W. Yin, C. H. Tang, Q. B. Wen, X. Q. Yang, and D. B. Yuan, “The relationships between physicochemical properties and conformational features of succinylated and acetylated kidney bean (Phaseolus vulgaris L.) protein isolates,” Food Research International, vol. 43, no. 3, pp. 730–738, 2010. View at Publisher · View at Google Scholar · View at Scopus
  21. S. W. Yin, C. H. Tang, Q. B. Wen, and X. Q. Yang, “Effects of acylation on the functional properties and In vitro trypsin digestibility of red kidney bean (Phaseolus vulgaris L.) protein isolate,” Journal of Food Science, vol. 74, no. 9, pp. E488–E494, 2009. View at Publisher · View at Google Scholar · View at Scopus
  22. A. C. Hengge and R. L. Stein, “Role of protein conformational mobility in enzyme catalysis: acylation of α-chymotrypsin by specific peptide substrates,” Biochemistry, vol. 43, no. 3, pp. 742–747, 2004. View at Publisher · View at Google Scholar · View at Scopus
  23. W. Tao, M. Li, and C. Zhao, “Structure and properties of regenerated Antheraea pernyi silk fibroin in aqueous solution,” International Journal of Biological Macromolecules, vol. 40, no. 5, pp. 472–478, 2007. View at Publisher · View at Google Scholar · View at Scopus
  24. P. J. Lamothe and P. G. McCormick, “Influence of acidity on the reaction of ninhydrin with amino acids,” Analytical Chemistry, vol. 44, no. 4, pp. 821–825, 1972. View at Google Scholar · View at Scopus
  25. E. Goormaghtigh, J. M. Ruysschaert, and V. Raussens, “Evaluation of the information content in infrared spectra for protein secondary structure determination,” Biophysical Journal, vol. 90, no. 8, pp. 2946–2957, 2006. View at Publisher · View at Google Scholar · View at Scopus
  26. D. M. Byler and H. Susi, “Examination of the secondary structure of proteins by deconvolved FTIR spectra,” Biopolymers, vol. 25, no. 3, pp. 469–487, 1986. View at Google Scholar · View at Scopus
  27. P. Innocenzi, L. Malfatti, A. Marcelli, and M. Piccinini, “Evaporation-induced crystallization of pluronic F127 studied in situ by time-resolved infrared spectroscopy,” Journal of Physical Chemistry A, vol. 114, no. 1, pp. 304–308, 2010. View at Publisher · View at Google Scholar · View at Scopus