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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Zou et al. (2001) studied this question.