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.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
