Some polypeptides encoded by the C-terminal region of human tropoelastin gene have been demonstrated to be amyloidogenic in vitro. The biological relevance of this finding is still under investigation given that only limited evidence concerning the involvement of elastin in amyloidosis exists. Recent studies identified, by mass spectrometry, several elastin fragments produced from the cleavages made by some elastases in human elastin substrate. Some of these fragments are contained into the same polypeptide sequences previously demonstrated to be amyloidogenic. Our hypothesis is that the up-regulation of elastases in inflammatory processes triggered, for example, by aging induces the release of elastin fragments potentially amyloidogenic. Therefore our aim in this study is to demonstrate if any of these fragments is amyloidogenic in vitro. At molecular level, CD, NMR, FTIR spectroscopies and MD simulations were used, while, at supramolecular level, Congo red binding assay and ThT fluorescence spectroscopy complemented with AFM microscopy were carried out. Our results show that the longest peptide, among those synthesized and mimicking the elastin fragments produced by elastases on human elastin, constituted of 22 residues, is able to aggregate into amyloid-like fibres. These findings support the hypothesis of amyloidogenesis of proteolytic fragments of elastin.