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Molecular and Supramolecular Structural Studies on Human Tropoelastin Sequences

Department of Chemistry, University of Basilicata, Potenza, Italy

Correspondence: Address reprint requests to A. M. Tamburro, Tel.: 39-0-971-202242; E-mail: antonio.tamburro{at}unibas.it.

One of the unusual properties of elastin is its ability to coacervate, which has been proposed to play an important role in the alignment of monomeric elastin for cross-linking into the polymeric elastin matrix. The temperature at which this transition takes place depends on several factors including protein concentration, ionic strength, and pH. Previously, polypeptide sequences encoded by different exons of the human tropoelastin gene have been analyzed for their ability to coacervate and to self-assemble. Few of them were indeed able to coacervate and only one, that encoded by exon 30 (EX30), gave amyloid fibers. In this article, we report on two chemically synthesized peptides—a decapeptide and an octadecapeptide—whose sequences are contained in the longer EX30 peptide and on a polypeptide (EX1–7) of 125 amino-acid residues corresponding to the sequence coded by the exons 1–7 and on a polypeptide (EX2–7) of 99 amino-acid residues encoded by exons 2–7 of human tropoelastin obtained by recombinant DNA techniques. Molecular and supramolecular structural characterization of these peptides showed that a minimum sequence of 20 amino acids is needed to form amyloid fibers in the exon 30-derived peptides. The N-terminal region of mature tropoelastin (EX2–7) gives rise to a coacervate and forms elastinlike fibers, whereas the polypeptide sequence containing the signal peptide (EX1–7) forms mainly amyloid fibers. Circular dichroism spectra show that β-structure is ubiquitous in all the sequences studied, suggesting that the presence of a β-structure is a necessary, although not sufficient, requirement for the appearance of amyloid fibers.