title: Dual role of Cu²⁺ ions on the aggregation and degradation of soluble Aβ oligomers and protofibrils investigated by fluorescence spectroscopy and AFM.
abstract: The neuropathological character of copper(II) ions (Cu(2+)) upon interaction with soluble human amyloid-β(1-42) that subsequently generates senile plaques and/or reactive oxygen species (ROS) is considered as one of the very important features of Alzheimer's disease. The present study carried out by using fluorescence spectroscopy and atomic-force microscopy (AFM) indeed confirms the dual role played by Cu(2+), namely as mediator of protein aggregation and as generator of ROS leading to irreversible protein alteration, which most likely involve two distinct copper-binding sites. The AFM investigations clearly evidence the copper-induced aggregation of Aβ oligomers and protofibrils, while comparative fluorescence measurements with copper and zinc reveals the crucial involvement of redox-active copper in the generation of Aβ-cross-linked structures.
authors.affiliation: Departament de Química Inorgànica, Universitat de Barcelona, Martí i Franquès 1-11, 08028 Barcelona, Spain.
authors.forename: Silvia
authors.initials: S
authors.lastname: García
authors.forename: Cristina
authors.initials: C
authors.lastname: Cuscó
authors.forename: Rosa F
authors.initials: RF
authors.lastname: Brissos
authors.forename: Ester
authors.initials: E
authors.lastname: Torrents
authors.forename: Amparo
authors.initials: A
authors.lastname: Caubet
authors.forename: Patrick
authors.initials: P
authors.lastname: Gamez
mesh_terms: D016229:Amyloid beta-Peptides / Q000737:chemistry*; D003300:Copper / Q000737:chemistry*; D006801:Humans; D018625:Microscopy, Atomic Force; D012995:Solubility; D013050:Spectrometry, Fluorescence
chemical_list: D016229:Amyloid beta-Peptides; D003300:Copper