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. 1. Introduction The development of advanced biomaterials is often inspired by the biological self-assembling modules, where simple building blocks such as amino acids, nucleic acids, and lipids are able to form complex natural systems. Peptide-based nanostructure complexes represent an important way toward the production of ordered self-assembling nanostructures with variegated possible applications [1, 2]. The growing interest in protein-inspired bionanotechnology is based on the knowledge of different self-assembling processes involving proteins and peptides. One of the most ubiquitous self-assembly processes in nature is the hierarchical organization of protein monomers into long filaments bundles and networks of nanometric dimensions. Extracellular matrix proteins, such as elastin and collagen, are involved in different self-assembling processes, both producing well-defined fibrils and fibers with specific mechanical and supramolecular properties [3]. Among the proteins able to self-assemble, elastin and elastin-related polypeptides [4, 5] have peculiar characteristics with repetitive sequences of small size and complexity responsible for their self-assembling as well as for the elastic properties. Furthermore, according to their sequences, elastin peptides are able to self-assemble in two different aggregation patterns, the classical elastin-like and the amyloid-type, with mechanical properties tuned by the choice of the sequence building blocks [4]. The peculiar features of elastin-related polypeptides render them a special subject of interest, as bionanomaterial with “smart” behavior [6]. With the aim of exploring the possible use of elastin self-assembling peptides for
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