THERMAL SCIENCE
International Scientific Journal
Find this paper on
CONTROL OF THE GELATION PROCESS OF SILK FIBROIN SOLUTION
ABSTRACT
In the present study, silk fibroin solution was controlled through a simple shearing to accomplish the steady and rapid gelation process and the conformational transition. Antheraea yamamai silk fibroin was formed into hydrogels quicker than Bombyx mori silk fibroin on the same condition. Comparing with Bombyx mori silk fibroin, the rapid gelation of Antheraea yamamai silk fibroin was concerned with its alternate polyalanine-containing units which are tended to form the α-helix structures spontaneously. The entropic cost during the conformational transition to β-sheet is less than that from random coil to β-sheet.
KEYWORDS
PAPER SUBMITTED: 2014-03-20
PAPER REVISED: 2014-05-02
PAPER ACCEPTED: 2014-07-01
PUBLISHED ONLINE: 2015-01-04
DOI REFERENCE: https://doi.org/10.2298/TSCI1405587L
CITATION EXPORT: view in browser or download as text file
REFERENCES
[1] Collins, M. N., Birkinshaw, C., Morphology of Crosslinked Hyaluronic Acid Porous Hydrogels, J. Appl. Polym. Sci., 120 (2011), 2, pp. 1040-1049
[2] Floren, M. L., et al., Carbon Dioxide Induced Silk Protein Gelation for Biomedical Applications, Biomacromolecules, 13 (2012), 2, pp. 2060-2072
[3] Plaza, G. R., et al., Correlation between Processing Conditions, Microstructure and Mechanical Behavior in Regenerated Silkworm Silk Fibers, J. Polym. Sci., Part B: Pol. Phys., 50 (2012), 7, pp. 455-465
[4] Ruoslahti, E., et al., New Perspectives in Cell Adhesion: RGD and Integrins, Science, 238 (1987), 4826, pp. 491-497
[5] Bhattarai, N., et al., Chitosan-Based Hydrogels for Controlled, Localized Drug Delivery, Adv. Drug Deliv. Rev., 62 (2010), 1, pp. 83-99
[6] Yucel, T., et al., Vortex-Induced Injectable Silk Fibroin Hydrogels, Biophys. J., 97 (2009), 7, pp. 2044- 2050
[7] Wang, X. Q., et al., Sonication-Induced Gelation of Silk Fibroin for Cell Encapsulation, Biomaterials, 29 (2008), 8, pp. 1054-1064
[8] Numata, K., et al., Molecular Structure, and Cytotoxicity of Silk Hydrogels, Biomacromolecules, 12 (2011), 6, pp. 2137-2144
[9] Zheng, Z., Wei, Y., et al., Preparation of Regenerated Antheraea Yamamai Silk Fibroin Film and Controlled Molecular Conformation Changes by Aqueous Ethanol Treatment, J. Appl. Polym. Sci., 116 (2010), 1, pp. 461-467
[10] Hart, F. U., Hayer-Hart, M., Converging Concepts of Protein Folding in vitro and in vivo, Nat. Struct. Mol. Biol., 16 (2009), 6, pp. 574-581
[11] Vepari, C., Kaplan, D. L., Silk as a Biomaterial, Prog. Polym. Sci., 32 (2007), 8-9, pp. 991-1007
[12] Hardy, J. G., Scheibel, T. R., Silk-Inspired Polymers and Proteins, Biochem. Soc. T., 37 (2009), 4, pp. 677-681
[13] Lapointe, S. M., et al., QTAIM Study of an α-Helix Hydrogen Bond Network, J. Phys. Chem. B, 113 (2009), 31, pp. 10957-10964
[14] Ki, C. S., et al., Silk Protein as a Fascinating Biomedical Polymer: Structural Fundamentals and Applications, Macromol. Res., 17 (2009), 12, pp. 935-942
[15] Scott, K. A., et al., Conformational Entropy of Alanine versus Glycine in Protein Denatured States, Proc. Natl. Acad. Sci., 104 (2007), 8, pp. 2661-2666
PDF VERSION [DOWNLOAD]
© 2026 Society of Thermal Engineers of Serbia. Published by the Vinča Institute of Nuclear Sciences, National Institute of the Republic of Serbia, Belgrade, Serbia. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution-NonCommercial-NoDerivs 4.0 International licence


