The interaction between alkyl derivatives and elastin.
Elastin from bovine ligamentum nuchae is exposed to aqueous solutions of different alkyl sulfates and carboxylates (fatty acids). The substrates of alkyl chain lengths varying between C8 and C17 bind to the elastin, the more so the longer the alkyl chain. However, the presence of two (or more) double bonds in the chain obstructs the penetration into the elastin network. As a result of absorption the elastin swells. The rate of binding is determined from the swelling of an elastin strip, that is monitored using a cathetometer. The diffusion of the substrate in the elastin is slower the longer the alkyl chain. The binding is reversible so that the Gibbs energy involved can be derived from the absorption isotherm. The values for the Gibbs energy of binding may amount to some tens of kJ per mol of substrate, with an increment of -4 kJ mol-1 per CH2 group. From the influence of temperature it is concluded that the binding is entropically driven. This, as well as the observation that the glass transition temperature of elastin is not affected by the presence of the alkyl derivatives, suggests that the substrates are bound to the amino acid residues of the elastin, rather than to the polypeptide backbone. Stress-strain experiments reveal that the elasticity decreases markedly on swelling of the sample, irrespective of the type of substrate that is absorbed. The phenomena described in this paper may be similar to those that occur between fatty acids in blood and arterial elastin, which could be at the origin of the development of atherosclerosis.
D000042:Absorption; D055592:Biophysical Phenomena; D001703:Biophysics; D003902:Detergents; D004548:Elasticity; D004549:Elastin; D005227:Fatty Acids; D013463:Sulfuric Acid Esters
D003902:Detergents; D005227:Fatty Acids; D013463:Sulfuric Acid Esters; D004549:Elastin