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Swim bladder collagen forms hydrogel with macroscopic superstructure by diffusion induced fast gelation

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Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/63152

Title: Swim bladder collagen forms hydrogel with macroscopic superstructure by diffusion induced fast gelation
Authors: Mredha, Md. Tariful Islam Browse this author
Zhang, Xi Browse this author
Nonoyama, Takayuki Browse this author
Nakajima, Tasuku Browse this author
Kurokawa, Takayuki Browse this author
Takagid, Yasuaki Browse this author
Gong, Jian Ping Browse this author →KAKEN DB
Issue Date: 21-Oct-2015
Publisher: Royal Society of Chemistry
Journal Title: Journal of materials chemistry b
Volume: 3
Issue: 39
Start Page: 7658
End Page: 7666
Publisher DOI: 10.1039/c5tb00877h
Abstract: Marine collagen has been attracting attention as a medical material in recent times due to the low risk of pathogen infection compared to animal collagen. Type I collagen extracted from the swim bladder of Bester sturgeon fish has excellent characteristics such as high denaturation temperature, high solubility, low viscosity and an extremely fast rate to form large bundle of fibers under certain conditions. These specific characteristics of swim bladder collagen (SBC) permit us to create stable, disk shaped hydrogels with concentric orientation of collagen fibers by the controlled diffusion of neutral buffer through collagen solution at room temperature. However, traditionally used animal collagens, e.g. calf skin collagen (CSC) and porcine skin collagen (PSC), could not form any stable and oriented structure by this method. The mechanism of the superstructure formation of SBC by a diffusion induced gelation process has been explored. The fast fibrillogenesis rate of SBC causes a quick squeezing out of the solvent from the gel phase to the sol phase during gelation, which builds an internal stress at the gel-sol interface. The tensile stress induces the collagen molecules of the gel phase to align along the gel-sol interface direction to give this concentric ring-shaped orientation pattern. On the other hand, the slow fibrillogenesis rate of animal collagens due to the high viscosity of the solution does not favor the ordered structure formation. The denaturation temperature of SBC increases significantly from 31 degrees C to 43 degrees C after gelation, whereas that of CSC and PSC were found to increase a little. Rheology experiment shows that the SBC gel has storage modulus larger than 15 kPa. The SBC hydrogels with thermal and mechanical stability have potential as bio-materials for tissue engineering applications.
Type: article (author version)
URI: http://hdl.handle.net/2115/63152
Appears in Collections:生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 龔 剣萍 (Gong Jian Ping)

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