Changes in the physical structure and chain dynamics of elastin network in homocysteine-cultured arteries.
The thermal and dielectric properties of the elastin network were investigated in arteries cultured with physiological and pathological concentrations of homocysteine, an aminoacid responsible of histological impairments in human arteries. The physical structure of this amorphous protein was investigated by differential scanning calorimetry (DSC). To explore the molecular dynamics of the elastin network in the nanometer range, we used thermally stimulated currents (TSC), a dielectric technique running at low frequency, and measuring the dipolar reorientations in proteins subjected to a static electrical field. Combining DSC and TSC experiments reveals the molecular mobility of the proteins, both in the glassy state and in the liquid state. Significant differences are evidenced in the physical structure and relaxation behavior of elastin network in cultured arteries (physiological and pathological concentrations of homocysteine) and discussed.
Samouillan
Valérie
V
Laboratoire de Physique des Polymères, Institut Carnot, CIRIMAT UMR 5085, Université Paul Sabatier, 118 route de Narbonne, 31062 Toulouse Cedex04, France. vsamou@cict.fr
Lamy
Edouard
E
Dandurand
Jany
J
Foucault-Bertaud
Alexandrine
A
Chareyre
Corinne
C
Lacabanne
Colette
C
Charpiot
Philippe
P
D000818:Animals; D001158:Arteries / Q000378:metabolism*; D002152:Calorimetry, Differential Scanning / Q000379:methods; D004549:Elastin / Q000737:chemistry*; D055664:Electrochemical Techniques; D006710:Homocysteine / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D056004:Molecular Dynamics Simulation; D013552:Swine; D013696:Temperature; D046509:Tissue Culture Techniques / Q000295:instrumentation / Q000379:methods*
D006710:Homocysteine; D004549:Elastin