In this paper we demonstrate that the sequence encoded by exon 28 (EX28) of human tropoelastin gene is able to give amyloid-like fibrils. CD (circular dichroism) in solution and solid-state FTIR (Fourier transform infrared spectroscopy) spectroscopies have shown the presence of beta-sheet conformation. At the supramolecular level the fibers formed by EX28 peptide were investigated by AFM (atomic force microscopy) and ESEM (environmental scanning electron microscopy). A very big left-handed helix, 100 mu m long, is visible together with aggregates of different sizes, some of them being constituted by helically interwoven fibers. Furthermore, an additional AFM image of EX28 is shown where the ultrastructure found is somewhat reminiscent of a more or less retiform, film. These findings should be useful for designing proper elastin-inspired biomaterials.