Abstract

Abstract : Development of elastometric polypeptide biomaterials indicate that polypeptide elastic processes may be either a passive and simple case of resistance to and recovery from a mechanical deformation or an active and coupled case of development of a motive force by transduction: thermomechanical, chemomechanical or electromechanical. In the coupled case, a transition between two states of different degree of elasticity may be achieved by a change in temperature, a change in chemical potential or a change in electrical potential. Commonly it is the situation of the temperature of a thermal transition being shifted by a change in chemical or electrical potential. Preliminary data suggest that repeating peptide sequences of novel design can provide elements of each case and that the temperature for the underlying thermal transition can be widely varied. The basic elastomeric repeating sequences are the polypentapeptide (Val(1)-Pro(2)-Gly(3)-VAl(4)-Gly(5))n and the polytetrapeptide (Val(1)-Pro(2)-Gly(3)-Gly(4))n, and the inelastic polyhexapeptide (Val-Ala-Pro-Gly-Val-Gly)n can be introduced to improve strength and handling characteristics of the elastomer. Special experiments are examining the coupling of extension to dielectric response, and the temperature dependence of the development of the elastomeric state as a function of pH for 20% Glu(4) - polypentapeptide.

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