Polypentapeptide of elastin: Temperature dependence of ellipticity and correlation with elastomeric force

Abstract

Circular dichroism (CD) is used to follow the conformational changes that attend temperature dependent aggregation leading to the viscoelastic (coacervate) state of the polypentapeptide of elastin in water. Two concentrations are used, 2.3 mg/ml and 0.023 mg/ml. The former results in aggregates of a size that exhibit much particulate distortion of the CD spectra whereas the latter results in spectra that are relatively free of distortions. Given the CD spectra of the temperature dependent aggregation of the lower concentration, it is possible to show that the same conformational change is occurring at high concentration. The structure of the polypentapeptide is one of limited order below 20°C which undergoes an inverse temperature transition to a conformation characterized by a regularly recurring β-turn at 40°C. The temperature profile for the conformational change is compared to the temperature dependence of elastomeric force of γ-irradiation cross-linked polypentapeptide coacervate. The curves virtually superimpose. When there is little order, there is little elastomeric force and elastomeric force develops to a near maximal value as the repeating Type II β-turn conformation develops. Not only is the elastomeric state non-random, the more nearly random state has very little elasticity. These results are the inverse of expectations based on the classical theory of rubber elasticity.