科研之友
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摘要
Collagen fibril (CF) has been a hot research topic in biomedical materials and tissue engineering for decades, because of its excellent physicochemical properties and biological performance. In the paper, type I CF was successfully prepared with acid-enzyme hydrolysis method, which was characterized by atomic force microscope (AFM), infrared spectroscopic analysis (FTIR) and dynamic rheological property testing. AFM results showed that CF had a uniform size distribution, that is, 135 nm +/- 5.00 nm, and enjoyed the D cycle horizontally striped structure. Temperature variation also has an effect on CF structures. At 45 degrees C, significant changes took place in the secondary structure of collagen. Dynamic rheological results showed that CF thermotropism occurred at 45.59 degrees C. In addition, under 25 degrees C and at a concentration ranging from 0.5 mg/mL to 2.0 mg/mL, angular frequency growth increased elastic modulus and the liquid carrying factor of CF solution, and decreased complex viscosity and mechanical loss. The results provide a new and reliable theoretical foundation for processing, molding and application of natural CF.
