title: Tuning self-assembly in elastin-derived peptides.
abstract: 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.
authors: Department of Science, University of Basilicata, Via Ateneo Lucano 10, 85100 Potenza, Italy. brigida.bochicchio@unibas.it.
authors: Brigida
authors: B
authors: Bochicchio
authors: Antonietta
authors: A
authors: Pepe
authors: Maria
authors: M
authors: Crudele
authors: Nicolas
authors: N
authors: Belloy
authors: Stephanie
authors: S
authors: Baud
authors: Manuel
authors: M
authors: Dauchez
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D004549:Elastin / Q000737:chemistry*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry*; D058105:Polymerization; D011487:Protein Conformation
chemical_list: D010446:Peptide Fragments; D004549:Elastin