Effects of Clioquinol on Metal-Triggered Amyloid-β Aggregation Revisited

• Published in: Inorganic chemistry Vol. 48; no. 20; pp. 9596 - 9598
• Main Authors: Mancino, Allana M, Hindo, Sarmad S, Kochi, Akiko, Lim, Mi Hee
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 19.10.2009
• Subjects: Alzheimer Disease - drug therapy; Alzheimer Disease - metabolism; Amyloid beta-Peptides - chemistry; Amyloid beta-Peptides - metabolism; Chelating Agents - pharmacology; Clioquinol - pharmacology; Copper - metabolism; Humans; Metals - metabolism; Solubility; Zinc - metabolism
• ISSN: 0020-1669; 1520-510X
• DOI: 10.1021/ic9014256

Amyloid-β (Aβ) plaques are largely associated with the neuropathogenesis of Alzheimer’s disease (AD). Metal ions such as CuII and ZnII have been implicated as contributors to their formation and deposition. Metal chelators have been used to modulate metal-induced Aβ aggregation. The bidentate ligand clioquinol (CQ) presents an effective influence on metal-involved Aβ aggregation, which has been explained through its metal chelation and is generally monitored by fluorescence and turbidity assays in vitro. The studies herein, however, suggest that the effects of CQ on metal-driven Aβ aggregation may not be visualized accurately by both assays. Subsequently, the present work demonstrates that CQ is able to chelate metal ions from metal−Aβ species and to assist, in part, in the disaggregation of Aβ aggregates, but it could not completely hinder the progression of Aβ aggregation.