Add time:09/04/2019         Source:sciencedirect.com

Elastins encompass the class of protein-based materials derived from the sequence of tropoelastin, the major protein component of native elastic tissue in vertebrates. Biophysical studies of native tropoelastin and tropoelastin-derived sequences have provided insight into the structural mechanism that underlies the elastomeric mechanical response of the material in its native environment. Tropoelastin and elastin-derived polypeptide sequences display a thermally reversible phase transition above a lower critical solution temperature, Tt, which coincides with the development of elastomeric restoring force in the material. The functionally critical properties of native elastins can be recapitulated in polypeptides that are composed of concatenated sequences of oligopeptide repeat motifs derived from tropoelastin; the most common of which are the pentapeptide sequences (Val-Pro-Gly-Xaa-Gly). These elastin-mimetic polypeptides display a well-defined correlation between repeat sequence and macromolecular properties, which enables the creation of a wide variety of synthetic elastin analogues with tailorable biophysical and macromolecular properties. This information has guided the design of synthetic elastin-mimetic materials for novel applications in tissue engineering, surface modification, controlled delivery and release, environmental remediation, and protein purification. Moreover, biosynthetic methods have been developed that enable the preparation of elastin-mimetic protein polymers that comprise complex sequences of defined macromolecular architecture (i.e., length, composition, and sequence), including multiblock copolymers. Thus, biosynthetic elastin-mimetic polypeptides represent the best-characterized biologically derived smart materials that have been prepared and analyzed to date.

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