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Cu 2+ Inhibits the Aggregation of Amyloid β‐Peptide(1–42) in vitro
Author(s) -
Zou Jin,
Kajita Katsushi,
Sugimoto Naoki
Publication year - 2001
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/1521-3773(20010618)40:12<2274::aid-anie2274>3.0.co;2-5
Subject(s) - thioflavin , peptide , in vitro , chemistry , amyloid (mycology) , biophysics , fluorescence , atomic force microscopy , fluorescence microscope , biochemistry , biology , nanotechnology , pathology , medicine , materials science , alzheimer's disease , inorganic chemistry , physics , disease , quantum mechanics
A distinct biochemical role of Cu 2+ 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 Cu 2+ –Aβ(42) complex is responsible for the inhibition because it stabilizes the soluble form of Aβ(42) and controls the conformational transition ([Eq. (1)]; k i =[Aβ(42)][Cu 2+ ]/[Cu 2+ –Aβ(42)]).