title: Tetrapeptidic molecular hydrogels: self-assembly and co-aggregation with amyloid fragment Aβ1-40.
abstract: A new family of isomeric tetrapeptides containing aromatic and polar amino acid residues that are able to form molecular hydrogels following a smooth change in pH is described. The hydrogels have been studied by spectroscopic and microscopic techniques showing that the peptide primary sequence has an enormous influence on the self-assembly process. In particular, the formation of extended hydrophobic regions and the appearance of π-stacking interactions have been revealed as the driving forces for aggregation. Moreover, the interaction of these compounds with amyloid peptidic fragment Aβ1-40 has been studied and some of them have been shown to act as templates for the aggregation of this peptide into non-β-sheet fibrillar structures. These compounds could potentially be used for the capture of toxic, soluble amyloid oligomers.
authors: Departament de Química Inorgànica i Orgànica, Universitat Jaume I, 12071 Castelló (Spain), Fax: (+34) 964728214.
authors: Marta
authors: M
authors: Tena-Solsona
authors: Juan F
authors: JF
authors: Miravet
authors: Beatriu
authors: B
authors: Escuder
mesh_terms: D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000648:ultrastructure; D006801:Humans; D020100:Hydrogels / Q000737:chemistry* / Q000494:pharmacology*; D008958:Models, Molecular; D009842:Oligopeptides / Q000737:chemistry* / Q000494:pharmacology*; D010446:Peptide Fragments / Q000737:chemistry* / Q000648:ultrastructure; D017433:Protein Structure, Secondary / Q000187:drug effects*
chemical_list: D016229:Amyloid beta-Peptides; D020100:Hydrogels; D009842:Oligopeptides; D010446:Peptide Fragments; C078592:amyloid beta-protein (1-40)
keywords: aggregation; fibers; gels; peptides; self-assembly