Abstract

Collagen fibres may be changed by reaction with a Zr-Al-Ti complex both in structure and properties. Specifically the microstructure changes of collagen fibres have been investigated through X-Ray diffraction (XRD), atomic force microscope (AFM) and scanning electron microscope (SEM), accompanied by thermal stability analysis carried out with differential scanning calorimeter (DSC) and thermogravimetric analyzer (TG). Owing to the interactions brought about by the Zr-Al-Ti complex, the D-pattern of collagen fibres has been shortened from 67nm to around 57nm, while the feature triple helices have not been destroyed. Meanwhile, collagen fibres have obviously been wrapped by Zr-Al-Ti complex to form a tight membrane. These effects are due to the interactions between gaps in collagenʼs characteristic gap-overlap structure in D-pattern, as well as interactions between neighbouring collagen fibres laterally. The changes of structure led to different thermal stabilities. The thermal denaturation temperature has finally been improved from 66.4°C to 82.6°C, and residual weight increased from 25.02% to 33.36% in the temperature range of 50-800°C.