Comparison of chemical treatments on the chain dynamics and thermal stability of bovine pericardium collagen.

A new approach for the replacement of heart valves consists of obtaining an acellular matrix from animal aortic valves that performs mechanically, is nonantigenic, and is free from calcification and fibroblast proliferation. Novel biochemical treatments must be developed for this purpose. In this work, we focus on the characterization of collagen in acellular bovine cardiovascular tissues, fresh or glutaraldehyde treated, and stored in different solutions [phosphate-buffered saline (PBS), ethanol, octanol, and glutaraldehyde], to determine whether the resulting fibrous material is structurally preserved. The preservation of the triple helical structure of collagen is checked by differential scanning calorimetry (DSC), which is a well suited technique to analyze thermal transitions in proteins, such as denaturation. To get insight into the molecular dynamics of collagen in the nanometric range, we used thermally stimulated currents, a dielectric technique running at low frequency, that measure the dipolar reorientations in proteins submitted to a static electrical field. The combined use of these two techniques allowed us to evaluate the physical structure and conformation of collagen after the different chemical treatments. We have found that the glutaraldehyde treatment followed by octanol storage preserves the triple helical conformation of the polypeptidic chains of collagen, contrary to the ethanol and PBS storage that induce drastic changes in the thermal and dielectric behavior of the protein. Moreover, this particular chemical treatment stabilizes the collagen structure (shift toward high temperature of the collagen denaturation and stiffening of the chains by a cross-linking action) when compared to the control sample, and so could provide interesting fibrous material for the conception of bioprosthetic heart valve.