Affiliations: Department of Science, University of Basilicata, Potenza, Italy
Note:  Corresponding author: Brigida Bochicchio, Department of Science, University of Basilicata, Via Ateneo Lucano, 10, 85100 Potenza, Italy. Tel.: +39 0971 205481; Fax: +39 0971 205678; E-mail: email@example.com
Abstract: Elastic fibers are responsible for elasticity of organs and tissues in vertebrates. Elastin is the amorphous component of these complex biopolymers and is an insoluble, highly cross-linked, hydrophobic protein assembled from a soluble precursor called tropoelastin. In order to elucidate the detailed structure of human tropoelastin, the exon-by-exon chemical synthesis of all the polypeptide sequences of the protein was accomplished. Herein, we review some of the most relevant results obtained at molecular, by using CD and NMR spectroscopies, and supramolecular level mainly by TEM. The overall results obtained for each polypeptide let us to assembly the elastin puzzle and envisaging the whole structure of human tropoelastin. Analogous structural studies were carried out on some polypeptide sequences inspired to elastomeric proteins. These findings give useful insights into the elasticity mechanism of all elastomeric proteins. The knowledge can be exploited in the near future to design novel bioelastomers with tailored material properties for use in medicine and industry.
Keywords: Elastin, amyloid-like, polyproline II, transmission electron microscopy, circular dichroism, nuclear magnetic resonance