Basic thermoanalytical studies of insoluble collagen matrices.

Insoluble collagen has been utilized as a base material for parenteral drug carrier systems. Information on its physicochemical properties was obtained by focussing on thermoanalytical methods. On the way from the raw material to the matrices, the acidic aqueous dispersion represents an important intermediate state. DSC and FTIR revealed its complete denaturation at 43 degrees C. Dense homogeneous collagen matrices were prepared by air-drying at 25 degrees C and became denatured at 103.5 degrees C, far above normal storage temperatures. Dielectrical Thermal Analysis demonstrated transitions in the dielectrical storage and loss moduli, reflecting the dissipation of electrical energy and increased molecular mobility caused by collapse of the triple helical structure. Cross-linking of the collagen dispersion with glutaraldehyde induced no alteration in the thermoanalytical properties of dry matrices. However, in the swollen state, after incubation of the devices in phosphate buffer the transition temperature increased from 50 to 70 degrees C as cross-linking was intensified. This indicated stronger interactions between the collagen fibre structures. Dissolution tests with cytochrome c-loaded matrices showed that higher amounts of the model protein were trapped inside the matrices as more glutaraldehyde was added.