Polypentapeptide of Elastin: Temperature Dependence Correlation of Elastomeric Force and Dielectric Permittivity

Biochem Biophys Res Commun. 1984 Dec 28;125(3):1082-8. doi: 10.1016/0006-291x(84)91394-9.


The polypentapeptide of elastin, (L X Val1-L X Pro2-Gly3-L X Val4-Gly5)n, when gamma-irradiation cross-linked in the coacervate state, is shown by means of thermoelasticity data to be a relatively simple system on which to study polypeptide elasticity. Strikingly, the temperature dependence of the elastomeric force exhibited by cross-linked polypentapeptide coacervate is shown to be proportional to the temperature dependence of the dielectric permittivity of the polypentapeptide coacervate over the critical temperature range of 25 degrees C to 55 degrees C where the force increases five fold. This demonstrates that the mobility of dipolar elements are in large part responsible for the elastomeric force and that dielectric relaxation studies contain the potential for identifying the nature of the dynamic elements responsible for bioelasticity.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Chemical Phenomena
  • Chemistry, Physical
  • Elasticity
  • Elastin / analysis*
  • Electric Conductivity
  • Temperature


  • Elastin