Tuning self-assembly in elastin-derived peptidesElectronic supplementary information (ESI) available: Radius of gyration of peptides, 1H-NMR chemical shift assignments of polypeptides, and CD of (VGGVG)3 in TBS and in mixture TFE-H2O. See DOI: 10.1039/c5sm00072f

Elastin-derived peptides are gaining increasing interest as potential biomaterials. Previous studies have demonstrated that short elastin-derived peptides are able to self-assemble into fibrils as the entire elastin protein. The motif responsible for that is the XGGZG motif at least three-fold repeated. In this work we have synthesized and studied, at molecular and supramolecular levels, four pentadecapeptides obtained by switching the X and Z residue with leucine and/or valine. We found that the four peptides formed 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 in the motif is crucial in driving the self-aggregation. The aim of this work is to provide the basis for designing elastin-derived peptides with tunable supramolecular architecture. Elastin-derived peptides as bioinspired materials with predictable architectures.