Tuning self-assembly in elastin-derived peptides.
Fiche publication
Date publication
mars 2015
Auteurs
Membres identifiés du Cancéropôle Est :
Pr DAUCHEZ Manuel, Pr BAUD Stéphanie
Tous les auteurs :
Bochicchio B, Pepe A, Crudele M, Belloy N, Baud S, Dauchez M
Lien Pubmed
Résumé
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.
Référence
Soft Matter. 2015 Mar 26.