Characterisation of elastin and collagen in aortic bioprostheses |
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Authors: | Dr V Samouillan A Lamure E Maurel J Dandurand C Lacabanne F Ballarin M Spina |
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Institution: | (1) Laboratoire de Physique des Polymères, Université Paul Sabatier, Toulouse, France;(2) Istituto di Istologia, Universita degli Studi di Padova, Padova, Italy |
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Abstract: | 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°C, and collagen denaturation is observed around 230°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 lowtemperature relaxations observed in both collagen and elastin are associated with localised
motions, whereas the high-temperature modes are attributed to more delocalised 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 destabilising effect of this
detergent is highlighted. |
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Keywords: | Porcine aortic valves Bioprostheses Collagen Elastin Differential scanning calorimetry Thermostimulated currents |
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