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The Effect of Molecular Weight on the Gelation Behavior of Regenerated Silk Solutions

  • Cho, Hee-Jung (Department of Advanced Organic Materials Science and Engineering, Kyungpook National University) ;
  • Um, In-Chul (Department of Natural Fiber Science, Kyungpook National University)
  • Received : 2011.08.26
  • Accepted : 2011.09.06
  • Published : 2011.09.30

Abstract

The various molecular weight (MW) regenerated silk fibroins were prepared with different dissolution condition and the effect of MW on the gelation behavior of regenerated aqueous silk fibroin (SF) solution was investigated. The result of gelation time measurement indicated that the gelation of SF aqueous solution was accelerated by the increase of MW and SF concentration. When formic acid was added in SF aqueous solution, the gelation time of SFL and SFC30 aqueous solution showed a significant decreaseat 0.03% formic acid addition. In case of the lowest MW sample, SFC180, SF molecules became aggregated and precipitated without gelation after 28 days storage time. These findings indicate that MW control of SF can be utilized to control the gelation time of SF aqueous solution.

Keywords

References

  1. Cho HJ, Ki CS, Oh H, Lee KH, Um IC (2011) Solution properties and Structural Characteristics of Various Molecular Weight Regenerated Silk Fibroins Prepared by Different Dissolution Condition. In preparation.
  2. Haider ZA, Aria M, Hirabayashi K (1993) Mechanism of the gelation of fibroin solution. Biosci Biotechnol Biochem 57, 1910-1912. https://doi.org/10.1271/bbb.57.1910
  3. Kang GD, Nahm JH, Park JS, Moon JY, Cho CS, Yeo JH (2000) Effects of poloxamer on the gelation of silk fibroin. Macromol Rapid Commun 21,788-791. https://doi.org/10.1002/1521-3927(20000701)21:11<788::AID-MARC788>3.0.CO;2-X
  4. Ki CS, Kim JW, Oh HJ, Lee KH, Park YH (2007) The effect of residual silk sericin on the structure and mechanical property of regenerated silk filament. Int J Biol Macromol 41, 346- 353. https://doi.org/10.1016/j.ijbiomac.2007.05.005
  5. Ki CS, Park SY, Kim HJ, Jung HM, Woo KM, Lee JW, Park YH (2008) Development of 3-D nanofibrous fibroin scaffold with high porosity by electrospinning: implications for bone regeneration. Biotech Lett 30, 405-410. https://doi.org/10.1007/s10529-007-9581-5
  6. Kim J, Park J, Li C, Jin H, Valluzzi R, Kaplan DL (2004) Structure and properties of silk hydrogels. Biomacrmolecules 5, 786-792. https://doi.org/10.1021/bm0345460
  7. Kweon HY, Ha HC, Um IC, Park YH (2001) Physical properties of silk fibroin/chitosan blend films. J Appl Polym Sci 80, 928-934. https://doi.org/10.1002/app.1172
  8. Kweon HY, Yeo JH, Lee KG, Lee YW, Park YH, Nahm J, Cho C (2001) Effects of poloxamer on the gelation of silk sericin. Macromol Rapid Commun 21, 1302-1305. https://doi.org/10.1002/1521-3927(20001201)21:18<1302::AID-MARC1302>3.0.CO;2-6
  9. Mathur AB, Tonelli A, Rathke T, Hudson S (1997) The dissolution and characterization of Bombyxmori silk fibroinin calcium nitrate methanol solution and the regeneration of films. Biopolymers 42, 61-74. https://doi.org/10.1002/(SICI)1097-0282(199707)42:1<61::AID-BIP6>3.0.CO;2-#
  10. Meinel L, Hofmann S, Karageorgiou V, Kirker-Head C, McCool J, Gronowicz G, Zichner L, Langer R, Vunjak-Novakovic G, Kaplan DL (2005) The inflammatory responses to silk films in vitro and in vivo. Biomaterials 26, 147-155. https://doi.org/10.1016/j.biomaterials.2004.02.047
  11. Minoura N, Aiba S, Gotoh Y, Tsukada M, Imai Y (1995) Attachment and growth of cultured fibroblast cells on silk protein matrixes. J Biomed Mater Res 29, 1215-1221. https://doi.org/10.1002/jbm.820291008
  12. Nagarkar S, Nicolai T, Chsssenieux C, Lele A (2010) Structure and gelation mechanism of silk hydrogels. Phys Chem Chem Phys 12, 3834-3844. https://doi.org/10.1039/b916319k
  13. Sakabe H, Ito H, Miyamoto T, Noishiki, Ha WS (1989) In vivo blood compatibility of regenerated silk fibroin. Sen-i Gakkaishi 45, 487-490. https://doi.org/10.2115/fiber.45.11_487
  14. Sukigara S, Gandhi M, Ayutsede J, Micklus M, Ko F (2003) Regeneration of Bombyxmori silk by electrospinning. part 1: processing parameters and geometric properties. Polymer 44, 5721-5727. https://doi.org/10.1016/S0032-3861(03)00532-9
  15. Um IC, Ki CS, Kweon H, Lee GK, Ihm DW, Park YH (2004) Wet spinning of silk polymer: II. Effect of drawing on the structural characteristics and properties of filament. Int J Biol Macromol 34, 107-119. https://doi.org/10.1016/j.ijbiomac.2004.03.011
  16. Um IC, Kweon HY, Lee KG, Park YH (2003) The role of formic acid in solution stability and crystallization of silk protein polymer. Int J Biol Macromol 33, 203-213. https://doi.org/10.1016/j.ijbiomac.2003.08.004
  17. Wang XQ, Kluge JA, Leisk GG, Kaplan DL (2008) Sonicationinduced gelation of silk fibroin for cell encapsulation. Biomaterials 29, 1054-1064. https://doi.org/10.1016/j.biomaterials.2007.11.003
  18. Yoshimizu H, Asakura T (1990) Preparation and characterization of silk fibroin powder and its application to enzyme immobilization. J Appl Polym Sci 40, 127-134. https://doi.org/10.1002/app.1990.070400111

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