Table of Contents
Conference Papers in Science
Volume 2014 (2014), Article ID 214235, 4 pages
http://dx.doi.org/10.1155/2014/214235
Conference Paper

Molecular Determinants for the Self-Assembly of Elastin Peptides

Department of Science, University of Basilicata, Via Ateneo Lucano 10, 85100 Potenza, Italy

Received 5 March 2014; Accepted 7 August 2014; Published 21 August 2014

Academic Editor: Antonio Lepedda

This Conference Paper is based on a presentation given by Antonietta Pepe at “LIAC Meeting on Vascular Research 2013” held from 18 September 2013 to 21 September 2013 in Alghero, Italy.

Copyright © 2014 Brigida Bochicchio et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Elastin and elastin-related peptides have great potential in the biomaterial field, because of their peculiar mechanical properties and spontaneous self-assembling behavior. Depending on their sequences and under appropriate experimental conditions, they are able to self-assemble in different fiber morphologies, including amyloid-like fibers. In this work, we will review recent data on elastin peptides derived from exon 30-coded domain of human tropoelastin. This domain has been shown to be fundamental for the correct assembly of elastin. However, the N-terminal region forms amyloid-like fibers, while the C-terminal fragment forms elastin-like fibers. A rationale for the varied aggregation pattern has been sought in the molecular structure of the peptides. Minimal differences in the sequences, adopting alternative conformations, are shown to be responsible for the observed data.