References
- 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.
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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-#
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
Cited by
- Effect of molecular weight and concentration on crystallinity and post drawing of wet spun silk fibroin fiber vol.15, pp.1, 2014, https://doi.org/10.1007/s12221-014-0153-8
- Storage stability of silk solution for viscosity and electrospinnability vol.33, pp.2, 2016, https://doi.org/10.7852/ijie.2016.33.2.138
- In situ formation of silk-gelatin hybrid hydrogels for affinity-based growth factor sequestration and release vol.6, pp.115, 2016, https://doi.org/10.1039/C6RA22908E
- 실크 세리신의 구조와 성질에 대한 최근 연구동향 vol.55, pp.2, 2011, https://doi.org/10.7852/jses.2019.55.2.44
- Regenerated silk fibroin-based dressing modified with carnosine-bentonite nanosheets accelerates healing of second-degree burn wound vol.74, pp.10, 2011, https://doi.org/10.1007/s11696-020-01155-9
- Conformation Transition Kinetics of Silk Fibroin in Aqueous Solution Explored Using Circular Dichroism Spectroscopy vol.6, pp.8, 2011, https://doi.org/10.1002/slct.202004180