Coacervation and ion-binding studies on aortic elastin.

Abstract CD studies were carried out on porcine aortic elastin in solution and as the coacervate. As with elastin from bovine ligamentum nuchae, coacervation results in a marked conformational change; addition of sodium dodecyl sulfate to an aqueous solution of aortic elastin mimics the effect of coacervation; dissolution in trifluoroethanol most closely reproduces the coacervate CD pattern, and addition of CaCl 2 to the trifluoroethanol solution causes a conformational change demonstrating ion binding. The inverse temperature transition which is responsible for coacervate formation at body temperatures and the effect of sodium dodecyl sulfate and trifluoroethanol in producing the coacervate CD pattern in solution suggests that hydrophobic interactions are important in the ordered association of α-elastin molecules to form the coacervate.