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Updated: Feb 11, 2026

Preparation of Oligomeric β-amyloid1-42 and Induction of Synaptic Plasticity Impairment on Hippocampal Slices
Published on: July 14, 2010
Cu2+ Inhibits the Aggregation of Amyloid β-Peptide(1-42) in vitro
Jin Zou1, Katsushi Kajita1, Naoki Sugimoto1
1Department of Chemistry Faculty of Science and Engineering Konan University 8-9-1 Okamoto, Higashinada-ku, Kobe 658-8501 (Japan) Fax: (+81) 78-435-2539.
Abstract:
A distinct biochemical role of Cu2+ as an inhibitor in the aggregation of the peptide Aβ(42) in vitro was revealed by thioflavin T fluorescence assay and atomic force microscopy. The Cu2+ -Aβ(42) complex is responsible for the inhibition because it stabilizes the soluble form of Aβ(42) and controls the conformational transition ([Eq. (1)]; ki =[Aβ(42)][Cu2+ ]/[Cu2+ -Aβ(42)]).
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