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 homocys- teine, an aminoacid responsible of histological impair- ments in human arteries. The physical structure of this amorphous protein was investigated by differential scan- ning calorimetry (DSC). To explore the molecular dynam- ics 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 reor- ientations in proteins subjected to a static electrical field. Combining DSC and TSC experiments reveals the molecu- lar 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 net- work in cultured arteries (physiological and pathological concentrations of homocysteine) and discussed.