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Trace copper(II) or zinc(II) ions drastically modify the aggregation behavior of amyloid-beta{1-42}: an AFM study

Innocenti, Massimo, Salvietti, Emanuele, Guidotti, Martina, Casini, Angela, Bellandi, Silvano, Foresti, Maria Luisa, Gabbiani, Chiara, Pozzi, Andrea, Zatta, Paolo and Messori, Luigi 2010. Trace copper(II) or zinc(II) ions drastically modify the aggregation behavior of amyloid-beta{1-42}: an AFM study. Journal of Alzheimer's Disease 19 (4) , pp. 1323-1329. 10.3233/JAD-2010-1338

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Abstract

Formation of amyloid-β (Aβ){1-42} amyloid fibrils, a characteristic feature of Alzheimer's disease (AD), was monitored in situ through atomic force microscopy (AFM). Well-structured amyloid fibrils slowly formed in solution within 24 hours for which high quality AFM pictures could be obtained. Remarkably, addition of either copper(II) or zinc(II) ions to the incubation medium, even at extremely low molar ratios, dramatically changed the Aβ {1-42} aggregation profile and prevented fibril formation. Aggregates of different morphology appeared in accordance with previous observations: small globular aggregates upon addition of zinc; ill-structured micro-aggregates in the case of copper. The implications of these AFM results are discussed in the context of current concepts for AD metallobiology.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Chemistry
Subjects: Q Science > QD Chemistry
Publisher: IOS Press
Date of Acceptance: 5 November 2009
Last Modified: 04 Jun 2017 08:30
URI: http://orca.cf.ac.uk/id/eprint/79347

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