Elastin-derived peptides as building-blocks for novel material functionalities

Elastin-derived peptides are gaining increasing interest as potential biomaterials. Short elastin-derived peptides are able to self-assemble in fibrils as the entire elastin protein. The motif responsible for that is the XGGZG motif at least three-fold repeated. Herein, we present four pentadecapeptides obtained by switching the X and Z residue with leucine and/or valine residue. This effect has been explored in the peptides at molecular and supramolecular level. We found that the four peptides gave rise to different supramolecular structures corresponding to specific molecular conformations. Our results show that not only the residue type but also the exact position occupied by the residue through the motif is crucial in driving the self-aggregation mechanism. The aim of this work is to put the basis for designing elastin–derived peptides with tunable supramolecular architecture tailored on the specific requirements that the final biomaterial must fulfill. These sequences are of outstanding interest as potential biomaterials for the simplicity of polymer design due to the presence of small-sized motifs. An interesting element of novelty is represented by the coniugation of elastin self-assembling peptides with carbohydrates and aminoglycoside antibiotics in order to construct 2D/3D scaffolds as smart biomaterials.