| Abstract: | It is suggested that the temperature-dependent swelling behavior of water-swollen elastin is due entirely to the interaction of the numerous nonpolar groups in the elastin protein wiht the aqueous swelling solvent (i.e., ahydrophobic interaction). Flory-Rehner theory for network swelling was used to test this hypothesis. Calculated values for the solvent–polymer interaction parameter, χ1, derived from swelling data indicate that water is a very poor solvent for elastin at all temperatures over the range 0–70° C. Comparison of the calculated χ1 values with theoretical values for the free energy of interaction of nonpolar solutes and water strongly suggests that the swelling behavior of elastin can be attributed quantitatively to hydrophobic interactions. The implications of these results for the structure and elastic mechanism of elastin are discussed. |
