Abstract

IThe collagen fibril (CF) is a hot topic in biomedical materials and tissue engineering research because of its physicochemical properties and biological performance. In this paper, Type I CF was successfully prepared by the acid-enzyme hydrolysis method. The samples prepared were subjected to atomic force microscope examination (AFM), infrared spectroscopic analysis (FTIR) and histological staining.

AFM and histological staining results showed that CF had uniform thickness with a diameter of 135nm ± 5.00nm, and enjoyed the D cycle horizontally banded structure that is typical in Type I CF. At 45°C, significant changes occur to the secondary structure of collagen, when the temperature reaches 60°C, the supramolecular networks and triple helical structures of CF are completely destroyed. The results provide new and reliable theoretical grounds for processing, moulding, and application.