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The degradation behavior of silk fibroin derived from different ionic liquid solvents

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DOI: 10.4236/ns.2013.56A002    5,230 Downloads   8,211 Views   Citations

ABSTRACT

Establishing an appropriate degradation rate is critical for tissue engineering scaffolds. In this study, the degradation rate of silk fibroin three-dimensional scaffolds was regulated by changing the molecular weight (MW) of the silk fibroin. The solubility of silk fibroin depends primarily on the ionic ability of the slovent to dissolve silk fibroin, therefore, we regulated the MW of the silk fibroin using LiBr, Ca(NO3)2 and CaCl2 to dissolve the silk fibers. SDS-PAGE analysis showed that the MW of the CaCl2-derived silk fibroin was lower than the MW produced using LiBr and Ca(NO3)2. In vitro and in vivo degradation results showed that the scaffolds prepared by low-MW silk fibroin were more rapidly degraded. Furthermore, FTIR and amino acid analysis suggested that the amorphous regions were preferentially degraded by Collagenase IA, while the SDS-PAGE and amino acid analysis indicated that the scaffolds were degraded into polypeptides (mainly at 10-30 kDa) and amino acids. Because the CaCl2-derived scaffolds contained abundant low MW polypeptides, inter-intramolecular entanglement and traversing of molecular chains in the crystallites reduced, which resulted in rapid degradation. The in vivo degradation results suggested that the degradation rate of the CaCl2-derived scaffolds was better matched to dermis regeneration, indicating that the degradation rate of silk fibroin can be effectively regulated by changing the MW to achieve a suitable dermal tissue regeneration rate.

Conflicts of Interest

The authors declare no conflicts of interest.

Cite this paper

You, R. , Zhang, Y. , Liu, Y. , Liu, G. and Li, M. (2013) The degradation behavior of silk fibroin derived from different ionic liquid solvents. Natural Science, 5, 10-19. doi: 10.4236/ns.2013.56A002.

References

[1] Drury, J.L. and Mooney, D.L. (2003) Hydrogels for tissue engineering: Scaffold design variables and applications. Biomaterials, 24, 4337-4351. doi:10.1016/S0142-9612(03)00340-5
[2] Mandal, B.B., Grinberg, A., Gil, E.S., Panilaitis, B. and Kaplan, D.L. (2012) High-strength silk protein scaffolds for bone repair. Proceedings of the National Academy of Sciences of the United States of America, 109, 7699-7704. doi:10.1073/pnas.1119474109
[3] Marelli, B., Alessandrino, A., Farè, S., Freddi, G., Mantovani, D. and Tanzi, M.C. (2010) Compliant electrospun silk fibroin tubes for small vessel bypass grafting. Acta Biomaterialia, 6, 4019-4026. doi:10.1016/j.actbio.2010.05.008
[4] Zhang, Q., et al. (2012) Preparation of uniaxial multi channel silk fibroin scaffolds for guiding primary neurons. Acta Biomaterialia, 8, 2628-2638. doi:10.1016/j.actbio.2012.03.033
[5] Foss, C., Merzari, E., Migliaresi, C. and Motta, A. (2013) Silk fibroin/hyaluronic acid 3D matrices for cartilage tissue engineering. Biomacromolecules, 14, 38-47. doi:10.1021/bm301174x
[6] Mandal, B.B., Park, S-H., Gil, E.S. and Kaplan, D.L. (2011) Multilayered silk scaffolds for meniscus tissue engineering. Biomaterials, 32, 639-651. doi:10.1016/j.biomaterials.2010.08.115
[7] Li, M., Ogisob, M. and Minoura, N. (2003) Enzymatic degradation behavior of porous silk fibroin sheets. Bio materials, 24, 357-365. doi:10.1016/S0142-9612(02)00326-5
[8] Horan, R.L., et al. (2005) In vitro degradation of silk fibroin. Biomaterials, 26, 3385-3393. doi:10.1016/j.biomaterials.2004.09.020
[9] Hu, Y., Zhang, Q., You, R., Wang, L. and Li, M. (2012) The relationship between secondary structure and bio degradation behavior of silk fibroin scaffolds. Advances in Materials Science and Engineering, 2012, Article ID: 185905.
[10] Arai, T., Freddi, G., Innocenti, R. and Tsukada, M. (2004) Biodegradation of Bombyx mori silk fibroin fibers and films. Journal of Applied Polymer Science, 91, 2383-2390. doi:10.1002/app.13393
[11] Zhao, C., Wu, X., Zhang, Q., Yan, S. and Li, M. (2011) Enzymatic degradation of Antheraea pernyi silk fibroin 3D scaffolds and fibers. International Journal of Bio logical Macromolecules, 48, 249-255. doi:10.1016/j.ijbiomac.2010.11.004
[12] Wang Y., et al. (2008) In vivo degradation of three-dimensional silk fibroin scaffolds. Biomaterials, 29, 3415-3428. doi:10.1016/j.biomaterials.2008.05.002
[13] Zhou, J., Cao, C., Ma, X., Hu, L., Chen, L. and Wang C. (2010) In vitro and in vivo degradation behavior of aqueous-derived electrospun silk fibroin scaffolds. Polymer Degradation and Stability, 95, 1679-1685. doi:10.1016/j.polymdegradstab.2010.05.025
[14] Yang, Y., et al. (2009) Degradation behaviors of nerve guidance conduits made up of silk fibroin in vitro and in vivo. Polymer Degradation and Stability, 94, 2213-2220. doi:10.1016/j.polymdegradstab.2009.09.002
[15] Numata, K., Cebe, P. and Kaplan, D.L. (2010) Mechanism of enzymatic degradation of beta-sheet crystals. Bio materials, 31, 2926-2933. doi:10.1016/j.biomaterials.2009.12.026
[16] Kim, K., et al. (2003) Control of degradation rate and hydrophilicity in electrospun non-woven poly(d,l-lactide) nanofiber scaffolds for biomedical applications. Biomaterials, 24, 4977-4985. doi:10.1016/S0142-9612(03)00407-1
[17] Park, T.G. (1994) Degradation of poly(d,l-lacticacid) microspheres: Effect of molecular weight. Journal of Controlled Release, 30, 161-173. doi:10.1016/0168-3659(94)90263-1
[18] Phillips, D.M., et al. (2004) Dissolution and regeneration of Bombyxmori silk fibroin using ionic liquids. Journal of the American Chemical Society, 126, 14350-14351. doi:10.1021/ja046079f
[19] Hu, X., Kaplan, D and Cebe, P. (2006) Determining beta sheet crystallinity in fibrous proteins by thermal analysis and infrared spectroscopy. Macromolecules, 39, 6161-6170. doi:10.1021/ma0610109
[20] Yan, S., et al. (2013) Silk fibroin/chondroitin sulfate/ hyaluronic acid ternary scaffolds for dermal tissue reconstruction. Acta Biomaterialia, 9, 6771-6782. doi:10.1016/j.actbio.2013.02.016
[21] Vepari, C. and Kaplan, D.L. (2007) Silk as a biomaterial. Progress in Polymer Science, 32, 991-1007. doi:10.1016/j.progpolymsci.2007.05.013
[22] Zhou, C.Z., Confalonieri, F., Jacquet, M., Perasso, R., Li, Z.G. and Janin, J. (2001) Silk fibroin: Structural implications of a remarkable amino acid sequence. Proteins: Structure, Function, and Bioinformatics, 44, 119-122.
[23] Inoue, S., Tanaka, K., Arisaka, F., Kimura, S., Ohtomo, K. and Mizuno, S. (2000) Silk fibroin of Bombyxmori is secreted, assembling a high molecular mass elementary unit consisting of H-chain, L-chain, and P25, with a 6:6:1 molar ratio. The Journal of Biological Chemistry, 275, 40517-40528. doi:10.1074/jbc.M006897200
[24] Mathur, A.B., Tonelli, A., Rathke, T. and Hudson, S. (1997) The dissolution and characterization of Bombyxmori silk fibroin in calcium nitrate-methanol solution and the regeneration of films. Biopolymers, 42, 61-74. doi:10.1002/(SICI)1097-0282(199707)42:1<61::AID-BIP6>3.0.CO;2-#
[25] Ha, S.-W., Park, Y.H. and Hudson, S.M. (2003) Dissolution of bombyxmori silk fibroin in the calcium nitrate tetrahydrate-methanol system and aspects of wet spinning of fibroin solution. Biomacromolecules, 4, 488-496. doi:10.1021/bm0255948
[26] Yamada, H., Nakao, H., Takasu., H, Takasu, Y. and Tsubouchi, K. (2001) Preparation of undegraded native molecular fibroin solution from silkworm cocoons. Materials Science and Engineering: C, 14, 41-46. doi:10.1016/S0928-4931(01)00207-7
[27] Cho, H.J., Ki, C.S., Oh, H., Lee, K.H. and Um, I.C. (2012) Molecular weight distribution and solution properties of silk fibroins with different dissolution conditions. International Journal of Biological Macromolecules, 51, 336-341. doi:10.1016/j.ijbiomac.2012.06.007
[28] Yan, S.Q., Zhao, C.X., Wu, X.F., Zhang, Q. and Li, M.Z. (2010) Gelation behavior of Antheraea pernyi silk fibroin. Science China Chemistry, 53, 535-541. doi:10.1007/s11426-010-0093-0
[29] Hearle, J.W.S. (1958) A fringed fibril theory of structure in crystalline polymers. Journal of Polymer Science, 28, 432-435. doi:10.1002/pol.1958.1202811722
[30] Seifter, S. and Harper, E. (1971) The enzymes. 3rd Edition, In: Boyer, P., Ed., Academic Press Inc., New York, 649.
[31] Katagata, Y., Kikuchi, A. and Shimura K. (1984) Characterization of the crystalline-region peptides prepared from the posterior silk gland fibroin. Journal of Sericultural Science of Japan, 53, 165-174.
[32] Katagata, Y., Kikuchi, A. and Shimura, K. (1984) Fractionation and characterization of the amorphous-region peptides of fibroin prepared from the posterior silk gland. Journal of Sericultural Science of Japan, 53, 226-236.

  
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