Development of Elastomeric Polypeptide Biomaterials
Annual rept. 1 Jun 1987-31 May 1988
ALABAMA UNIV IN BIRMINGHAM LAB OF MOLECULAR BIOPHYSICS
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The most significant accomplishment of the last year was the first demonstration of mechanochemical coupling chemomechanical transduction in synthetic polypeptides. The demonstration was achieved, not by copy of a known contractile protein but rather by a design based on a new principle of contraction which was derived independently of a known contractile protein. The new principle, described as chemical modulation of an inverse temperature transition, was derived from studies of the polypentapeptide of elastin, POLYVPGVG, and analogs. The goals of this project are to design, prepare and characterize novel elastomeric polymers comprised of repeating peptide sequences, primarily the elastin pentamer and analogs of it alone and combined with repeating related hexapeptides andor tetrapeptides. The purpose is to develop polymers with different elastic moduli and increased extension limits, polymers with different temperature ranges for their inverse temperature transitions over which elastomeric force dramatically changes, polymers in which different heat changes effect the large changes in elastomeric force, polymers with different intensities and frequencies of their dielectric relaxations and polymers with wider temperature ranges over which they function as nearly ideal elastomers. In the elastomer design, the dominant repeat units will be pentamers and tetramers. Hexamers and alanine-rich, lysine-containing cross-linking sequences will be used to fine-tune properties. Reprints.
- Polymer Chemistry