Abstract
Nano-SiO2 was immobilized onto dialdehyde cellulose (DAC) to prepare SiO2/DAC hybrid materials. Fourier transform infrared spectra (FTIR), thermogravimetric analysis and field emission scanning electron microscopy of SiO2/DAC indicated that nano-SiO2 had been successfully hybridized with DAC. X-ray diffraction suggested that the structure of DAC was influenced by the nano-SiO2. SiO2/DAC was then used as the cross-linker of collagen solutions. Gel electrophoresis patterns and FTIR reflected that cross-linking occurred between DAC and collagen, but that collagen retained the native triple-helix, respectively. Differential scanning calorimetry indicated that the thermal stability of collagen could be effectively improved by SiO2/DAC. Dynamic rheology tests revealed that the flowability of collagens cross-linked by SiO2/DAC was superior to that of those cross-linked by DAC; meanwhile, collagens cross-linked by SiO2/DAC possessed a more homogeneous morphology compared to those cross-linked by DAC. The hybridization of SiO2/DAC as a cross-linker for collagen could effectively prevent the gelation caused by excessive cross-linking, and significantly improve the thermostability of collagen, which could be helpful for collagen being applied in fields including biomaterials, cosmetics, etc.
Highlights
Collagen, the major component of extracellular matrices, has become a popular biomaterial and has been widely used in pharmacy, food, cosmetics and tissue engineering due to its bioactivity, biocompatibility and biodegradability [1,2,3]
A novel cross-linking agent of collagen was prepared via the hybridization of dialdehyde cellulose (DAC) and nano-SiO2
SiO2/DAC hybrid materials were added into collagen solutions
Summary
The major component of extracellular matrices, has become a popular biomaterial and has been widely used in pharmacy, food, cosmetics and tissue engineering due to its bioactivity, biocompatibility and biodegradability [1,2,3]. Aqueous preparations of collagen can be used for medial injection [4] or used as drug carriers and so on [5,6]; collagen solutions may be processed into a variety of formats, including sheets, fibers, sponges and packaging films [7,8,9,10]. During these applications and processes, the thermal stability of collagen in solutions plays an essential role in keeping collagen against denaturation, as the excellent characteristics of the native collagen would be lost if the collapse of the triple helix to a random coil occurred.
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