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.
Highlights
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
Mw (Da) 1961.2 1324.5 1421.6 derived from the exon 30-coded domain of human tropoelastin (EX30), able to form amyloid-like fibers, with the aim of identifying the molecular determinants for the varied self-assembly of elastin peptides
In this paper, we analyzed the influence of the molecular structure in defining the aggregation pattern of two closely related elastin peptides
Summary
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. One of the most ubiquitous selfassembly 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 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]. We will review the main results obtained on two of these fragments
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