Trace copper(II) or zinc(II) ions drastically modify the aggregation behavior of Amyloid-β1-42: An AFM study

Massimo Innocenti; Emanuele Salvietti; Martina Guidotti; Angela Casini; Silvano Bellandi; Maria Luisa Foresti; Chiara Gabbiani; Andrea Pozzi; Paolo Zatta; Luigi Messori

doi:10.3233/JAD-2010-1338

Trace copper(II) or zinc(II) ions drastically modify the aggregation behavior of Amyloid-β1-42: An AFM study

Massimo Innocenti, Emanuele Salvietti, Martina Guidotti, Angela Casini, Silvano Bellandi, Maria Luisa Foresti, Chiara Gabbiani, Andrea Pozzi, Paolo Zatta, Luigi Messori

Research output: Contribution to journal › Article › peer-review

77 Scopus citations

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 Aβ1-42 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.

Original language	English
Pages (from-to)	1323-1329
Number of pages	7
Journal	Journal of Alzheimer's Disease
Volume	19
Issue number	4
DOIs	https://doi.org/10.3233/JAD-2010-1338
State	Published - 2010
Externally published	Yes

Keywords

Alzheimer's disease
Amyloid-β
Atomic force microscopy
Metal ions

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.3233/JAD-2010-1338

Cite this

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title = "Trace copper(II) or zinc(II) ions drastically modify the aggregation behavior of Amyloid-β1-42: An AFM study",

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 Aβ1-42 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.",

keywords = "Alzheimer's disease, Amyloid-β, Atomic force microscopy, Metal ions",

author = "Massimo Innocenti and Emanuele Salvietti and Martina Guidotti and Angela Casini and Silvano Bellandi and Foresti, {Maria Luisa} and Chiara Gabbiani and Andrea Pozzi and Paolo Zatta and Luigi Messori",

year = "2010",

doi = "10.3233/JAD-2010-1338",

language = "English",

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T1 - Trace copper(II) or zinc(II) ions drastically modify the aggregation behavior of Amyloid-β1-42

T2 - An AFM study

AU - Innocenti, Massimo

AU - Salvietti, Emanuele

AU - Guidotti, Martina

AU - Casini, Angela

AU - Bellandi, Silvano

AU - Foresti, Maria Luisa

AU - Gabbiani, Chiara

AU - Pozzi, Andrea

AU - Zatta, Paolo

AU - Messori, Luigi

PY - 2010

Y1 - 2010

N2 - 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 Aβ1-42 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.

AB - 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 Aβ1-42 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.

KW - Alzheimer's disease

KW - Amyloid-β

KW - Atomic force microscopy

KW - Metal ions

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DO - 10.3233/JAD-2010-1338

M3 - Article

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VL - 19

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EP - 1329

JO - Journal of Alzheimer's Disease

JF - Journal of Alzheimer's Disease

IS - 4

ER -

Trace copper(II) or zinc(II) ions drastically modify the aggregation behavior of Amyloid-β1-42: An AFM study

Abstract

Keywords

UN SDGs

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