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Tetrapeptidic Molecular Hydrogels: Self‐assembly and Co‐aggregation with Amyloid Fragment Aβ1‐40
Author(s) -
TenaSolsona Marta,
Miravet Juan F.,
Escuder Beatriu
Publication year - 2014
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201302651
Subject(s) - self healing hydrogels , chemistry , peptide , stacking , amyloid (mycology) , self assembly , amyloid fibril , beta sheet , hydrophobic effect , fibril , biophysics , sequence (biology) , peptide sequence , amino acid , fragment (logic) , molecular dynamics , stereochemistry , polymer chemistry , biochemistry , amyloid β , organic chemistry , computational chemistry , biology , medicine , inorganic chemistry , disease , pathology , gene , computer science , programming language
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.