Tetrapeptidic Molecular Hydrogels: Self-assembly and Co-aggregation with Amyloid Fragment Aβ1-40
comunitat-uji-handle:10234/9
comunitat-uji-handle2:10234/7053
comunitat-uji-handle3:10234/8639
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http://dx.doi.org/10.1002/chem.201400346 |
Metadatos
Título
Tetrapeptidic Molecular Hydrogels: Self-assembly and Co-aggregation with Amyloid Fragment Aβ1-40Fecha de publicación
2014-01Editor
WILEY-VCH Verlag GmbH & Co. KGaAISSN
0947-6539; 1521-3765Tipo de documento
info:eu-repo/semantics/articleVersión de la editorial
http://onlinelibrary.wiley.com/doi/10.1002/chem.201302651/fullPalabras clave / Materias
Resumen
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 ... [+]
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. [-]
Publicado en
Chemistry - A European Journal Vol. 20, no. 4, 2014Derechos de acceso
Copyright © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
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info:eu-repo/semantics/restrictedAccess
http://rightsstatements.org/vocab/InC/1.0/
info:eu-repo/semantics/restrictedAccess
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