About this Journal Submit a Manuscript Table of Contents
BioMed Research International
Volume 2013 (2013), Article ID 904314, 13 pages
http://dx.doi.org/10.1155/2013/904314
Research Article

Preliminary Characterization of Genipin-Cross-Linked Silk Sericin/Poly(vinyl alcohol) Films as Two-Dimensional Wound Dressings for the Healing of Superficial Wounds

1Bioactive Resources for Innovative Clinical Applications Research Unit, Chulalongkorn University, Phayathai Road, Pathumwan, Bangkok 10330, Thailand
2Department of Pharmacy Practice, Faculty of Pharmaceutical Sciences, Chulalongkorn University, Phayathai Road, Pathumwan, Bangkok 10330, Thailand
3Department of Chemical Engineering, Faculty of Engineering, Chulalongkorn University, Phayathai Road, Pathumwan, Bangkok 10330, Thailand
4Department of Pharmaceutical Technology and Drug Delivery System Excellence Center, Faculty of Pharmaceutical Sciences, Prince of Songkla University, Hat Yai, Songkhla 90110, Thailand

Received 9 May 2013; Accepted 7 August 2013

Academic Editor: Joshua R. Mauney

Copyright © 2013 Tippawan Siritientong 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. R. Okabayashi, M. Nakamura, T. Okabayashi, Y. Tanaka, A. Nagai, and K. Yamashita, “Efficacy of polarized hydroxyapatite and silk fibroin composite dressing gel on epidermal recovery from full-thickness skin wounds,” Journal of Biomedical Materials Research, vol. 90, no. 2, pp. 641–646, 2009. View at Publisher · View at Google Scholar · View at Scopus
  2. L. Cuttle, M. Kempf, G. E. Phillips et al., “A porcine deep dermal partial thickness burn model with hypertrophic scarring,” Burns, vol. 32, no. 7, pp. 806–820, 2006. View at Publisher · View at Google Scholar · View at Scopus
  3. N. S. Gibran, S. Boyce, and D. G. Greenhalgh, “Cutaneous wound healing,” Journal of Burn Care and Research, vol. 28, no. 4, pp. 577–579, 2007. View at Publisher · View at Google Scholar · View at Scopus
  4. P. Aramwit and A. Sangcakul, “The effects of sericin cream on wound healing in rats,” Bioscience, Biotechnology and Biochemistry, vol. 71, no. 10, pp. 2473–2477, 2007. View at Publisher · View at Google Scholar · View at Scopus
  5. P. Aramwit, S. Kanokpanont, T. Nakpheng, and T. Srichana, “The effect of sericin from various extraction methods on cell viability and collagen production,” International Journal of Molecular Sciences, vol. 11, no. 5, pp. 2200–2211, 2010. View at Publisher · View at Google Scholar · View at Scopus
  6. P. Aramwit, S. Kanokpanont, W. De-Eknamkul, K. Kamei, and T. Srichana, “The effect of sericin with variable amino-acid content from different silk strains on the production of collagen and nitric oxide,” Journal of Biomaterials Science, Polymer Edition, vol. 20, no. 9, pp. 1295–1306, 2009. View at Publisher · View at Google Scholar · View at Scopus
  7. S. C. Kundu, B. C. Dash, R. Dash, and D. L. Kaplan, “Natural protective glue protein, sericin bioengineered by silkworms: potential for biomedical and biotechnological applications,” Progress in Polymer Science, vol. 33, no. 10, pp. 998–1012, 2008. View at Publisher · View at Google Scholar · View at Scopus
  8. B. B. Mandal, A. S. Priya, and S. C. Kundu, “Novel silk sericin/gelatin 3-D scaffolds and 2-D films: fabrication and characterization for potential tissue engineering applications,” Acta Biomaterialia, vol. 5, no. 8, pp. 3007–3020, 2009. View at Publisher · View at Google Scholar · View at Scopus
  9. B. C. Dash, B. B. Mandal, and S. C. Kundu, “Silk gland sericin protein membranes: fabrication and characterization for potential biotechnological applications,” Journal of Biotechnology, vol. 144, no. 4, pp. 321–329, 2009. View at Publisher · View at Google Scholar · View at Scopus
  10. M. Sasaki, Y. Kato, H. Yamada, and S. Terada, “Development of a novel serum-free freezing medium for mammalian cells using the silk protein sericin,” Biotechnology and Applied Biochemistry, vol. 42, no. 2, pp. 183–188, 2005. View at Publisher · View at Google Scholar · View at Scopus
  11. K. Tsubouchi, Y. Igarashi, Y. Takasu, and H. Yamada, “Sericin enhances attachment of cultured human skin fibroblasts,” Bioscience, Biotechnology and Biochemistry, vol. 69, no. 2, pp. 403–405, 2005. View at Publisher · View at Google Scholar · View at Scopus
  12. S. Terada, T. Nishimura, M. Sasaki, H. Yamada, and M. Miki, “Sericin, a protein derived from silkworms, accelerates the proliferation of several mammalian cell lines including a hybridoma,” Cytotechnology, vol. 40, no. 1–3, pp. 3–12, 2003. View at Publisher · View at Google Scholar · View at Scopus
  13. F. Zhang, Z. Zhang, X. Zhu, E. T. Kang, and K. G. Neoh, “Silk-functionalized titanium surfaces for enhancing osteoblast functions and reducing bacterial adhesion,” Biomaterials, vol. 29, no. 36, pp. 4751–4759, 2008. View at Publisher · View at Google Scholar · View at Scopus
  14. R. Dash, M. Mandal, S. K. Ghosh, and S. C. Kundu, “Silk sericin protein of tropical tasar silkworm inhibits UVB-induced apoptosis in human skin keratinocytes,” Molecular and Cellular Biochemistry, vol. 311, no. 1-2, pp. 111–119, 2008. View at Publisher · View at Google Scholar · View at Scopus
  15. P. Aramwit, T. Siritientong, S. Kanokpanont, and T. Srichana, “Formulation and characterization of silk sericin-PVA scaffold crosslinked with genipin,” International Journal of Biological Macromolecules, vol. 47, no. 5, pp. 668–675, 2010. View at Publisher · View at Google Scholar · View at Scopus
  16. J. S. Yoo, Y. J. Kim, S. H. Kim, and S. H. Choi, “Study on genipin: a new alternative natural crosslinking agent for fixing heterograft tissue,” Korean Journal of Thoracic and Cardiovascular Surgery, vol. 44, no. 3, pp. 197–207, 2011. View at Publisher · View at Google Scholar · View at Scopus
  17. T. Siritientong, T. Srichana, and P. Aramwit, “The effect of sterilization methods on the physical properties of silk sericin scaffolds,” AAPS PharmSciTech, vol. 12, no. 2, pp. 771–781, 2011. View at Publisher · View at Google Scholar · View at Scopus
  18. K. Lee, H. Kweon, J. H. Yeo et al., “Effect of methyl alcohol on the morphology and conformational characteristics of silk sericin,” International Journal of Biological Macromolecules, vol. 33, no. 1–3, pp. 75–80, 2003. View at Publisher · View at Google Scholar · View at Scopus
  19. W. A. Bubnis and C. M. Ofner III, “The determination of ε-amino groups in soluble and poorly soluble proteinaceous materials by a spectrophotometric method using trinitrobenzenesulfonic acid,” Analytical Biochemistry, vol. 207, no. 1, pp. 129–133, 1992. View at Publisher · View at Google Scholar · View at Scopus
  20. J. Zhou, J. Zhang, Y. Ma, and J. Tong, “Surface photo-crosslinking of corn starch sheets,” Carbohydrate Polymers, vol. 74, no. 3, pp. 405–410, 2008. View at Publisher · View at Google Scholar · View at Scopus
  21. L. Greenspan, “Humidity fixed points of binary saturated aqueous solutions,” Journal of Research of the National Bureau of Standards A, vol. 81, no. 1, pp. 89–96, 1977. View at Scopus
  22. T. Mosmann, “Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays,” Journal of Immunological Methods, vol. 65, no. 1-2, pp. 55–63, 1983. View at Scopus
  23. J. Kong and S. Yu, “Fourier transform infrared spectroscopic analysis of protein secondary structures,” Acta Biochimica et Biophysica Sinica, vol. 39, no. 8, pp. 549–559, 2007. View at Publisher · View at Google Scholar · View at Scopus
  24. I. R. Rodrigues, M. M. de Camargo Forte, D. S. Azambuja, and K. R. L. Castagno, “Synthesis and characterization of hybrid polymeric networks (HPN) based on polyvinyl alcohol/chitosan,” Reactive and Functional Polymers, vol. 67, no. 8, pp. 708–715, 2007. View at Publisher · View at Google Scholar · View at Scopus
  25. E. N. Hidawati and A. M. Mimi Sakinah, “Treatment of glycerin pitch from biodiesel production,” International Journal of Chemical and Environmental Engineering, vol. 2, pp. 309–313, 2011.
  26. W. H. Chang, Y. Chang, P. H. Lai, and H. W. Sung, “A genipin-crosslinked gelatin membrane as wound-dressing material: in vitro and in vivo studies,” Journal of Biomaterials Science, Polymer Edition, vol. 14, no. 5, pp. 481–495, 2003. View at Publisher · View at Google Scholar · View at Scopus
  27. D. I. Lee, “The effects of latex coalescence and interfacial crosslinking on the mechanical properties of latex films,” Polymer, vol. 46, no. 4, pp. 1287–1293, 2005. View at Publisher · View at Google Scholar · View at Scopus
  28. Y. Huang, H. Yu, and C. Xiao, “Effects of Ca2+ crosslinking on structure and properties of waterborne polyurethane-carboxymethylated guar gum films,” Carbohydrate Polymers, vol. 66, no. 4, pp. 500–513, 2006. View at Publisher · View at Google Scholar · View at Scopus
  29. S. Benavides, R. Villalobos-Carvajal, and J. E. Reyes, “Physical, mechanical and antibacterial properties of alginate film: effect of the crosslinking degree and oregano essential oil concentration,” Journal of Food Engineering, vol. 110, no. 2, pp. 232–239, 2011. View at Publisher · View at Google Scholar · View at Scopus
  30. J. W. Rhim, “Physical and mechanical properties of water resistant sodium alginate films,” Food Science and Technology, vol. 37, no. 3, pp. 323–330, 2004. View at Publisher · View at Google Scholar · View at Scopus
  31. D. W. Hutmacher, “Scaffold design and fabrication technologies for engineering tissues—state of the art and future perspectives,” Journal of Biomaterials Science, Polymer Edition, vol. 12, no. 1, pp. 107–124, 2001. View at Publisher · View at Google Scholar · View at Scopus
  32. A. Hasimi, A. Stavropoulou, K. G. Papadokostaki, and M. Sanopoulou, “Transport of water in polyvinyl alcohol films: effect of thermal treatment and chemical crosslinking,” European Polymer Journal, vol. 44, no. 12, pp. 4098–4107, 2008. View at Publisher · View at Google Scholar · View at Scopus
  33. J. Ratanavaraporn, H. Furuya, H. Kohara, and Y. Tabata, “Synergistic effects of the dual release of stromal cell-derived factor-1 and bone morphogenetic protein-2 from hydrogels on bone regeneration,” Biomaterials, vol. 32, no. 11, pp. 2797–2811, 2011. View at Publisher · View at Google Scholar · View at Scopus
  34. C. Nathan, “Inducible nitric oxide synthase: what difference does it make?” Journal of Clinical Investigation, vol. 100, no. 10, pp. 2417–2423, 1997. View at Scopus
  35. M. B. Witte, F. J. Thornton, D. T. Efron, and A. Barbul, “Enhancement of fibroblast collagen synthesis by nitric oxide,” Nitric Oxide, vol. 4, no. 6, pp. 572–582, 2000. View at Publisher · View at Google Scholar · View at Scopus
  36. D. Miljkovic, I. Cvetkovic, S. Stosic-Grujicic, and V. Trajkovic, “Mycophenolic acid inhibits activation of inducible nitric oxide synthase in rodent fibroblasts,” Clinical and Experimental Immunology, vol. 132, no. 2, pp. 239–246, 2003. View at Publisher · View at Google Scholar · View at Scopus
  37. M. Du, M. M. Islam, L. Lin, Y. Ohmura, Y. Moriyama, and S. Fujimura, “Promotion of proliferation of murine BALB/c 3T3 fibroblasts mediated by nitric oxide at lower concentrations,” Biochemistry and Molecular Biology International, vol. 41, no. 3, pp. 625–631, 1997. View at Scopus
  38. D. T. Efron, S. J. Kirk, M. C. Regan, H. L. Wasserkrug, and A. Barbul, “Nitric oxide generation from L-arginine is required for optimal human peripheral blood lymphocyte DNA synthesis,” Surgery, vol. 110, no. 2, pp. 327–334, 1991. View at Scopus