Characterisation of elastin and collagen in aortic bioprostheses.
Porcine aortic valves used as cardiac valve bioprostheses are well adapted to physiological functions in the short term, but they lack long-term durability. Several multi-step extractions have been performed to obtain a perfectly acellular matrix. A new physical methodology is proposed to evaluate the resulting fibrous protein damage after biochemical extraction (TRI-COL and SDS). Thermal analysis techniques are adapted to collagen and elastin characterisation in the solid state. The aortic tissue thermal transitions are determined by differential scanning calorimetry (DSC): elastin glass transition is observed around 200 degrees C, and collagen denaturation is observed around 230 degrees C. These parameters are characteristic of the elastin network arrangement and of collagen triple-helix stability. The technique of thermostimulated currents (TSC) is well suited to specify the chain dynamics of proteins. The low-temperature relaxations observed in both collagen and elastin are associated with localised motions, whereas the high-temperature modes are attributed to more delocalized motions of the chains. Therefore TSC and DSC spectrometries allow physical parameters specific to collagen and elastin to be obtained and their interaction in aortic tissues to be determined. According to the significant evolution of these parameters on SDS samples, the destabilizing effect of this detergent is highlighted.
Samouillan
V
V
Laboratoire de Physique des Polymères, Université Paul Sabatier, Toulouse, France. vsamou@cict.fr
Lamure
A
A
Maurel
E
E
Dandurand
J
J
Lacabanne
C
C
Ballarin
F
F
Spina
M
M
D000818:Animals; D001705:Bioprosthesis; D002152:Calorimetry, Differential Scanning; D003094:Collagen / Q000737:chemistry*; D004549:Elastin / Q000737:chemistry*; D006350:Heart Valve Prosthesis; D006801:Humans; D013696:Temperature
D003094:Collagen; D004549:Elastin