HAp protein composites formed by hydrolysis of α-TCP

Composite material composed of hydroxyapatite (HAp) and structural proteins, such as type I collagen or cross-linked gelatins, were synthesized at 37.4 degrees C by hydrolysis of alpha tricalcium phosphate (alpha-TCP) in the presence of these protein structures. X-ray diffraction (XRD) and isothermal calorimetry were used as tools to evaluate the rate of HAp formation. Rates of HAp formation depend on protein structure. Gelatin enhances HAp formation while collagen delays it. Changes in pH during the hydrolysis alpha-TCP are unlikely to have an aggressive effect on the surrounding tissue. The presence of the protein improves the ductility of the HAp/protein composite but it decreases the tensile strength.