ArticleBiochemistry2013
The elevated copper binding strength of amyloid-β aggregates allows the sequestration of copper from albumin: a pathway to accumulation of copper in senile plaques.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 63 citations in OpenAlex.
- Copper homeostasis and cuproptosis in Alzheimer's disease (Review).International journal of molecular medicine · 2025Review
- Discovery of powerful multifaceted antioxidant for combating oxidative stress associated with neurodegenerative disorders.Acta pharmaceutica Sinica. B · 2025Article
- Perturbations in levels of essential metals less severe in Parkinson's disease without dementia than in Parkinson's disease dementia.Metallomics : integrated biometal science · 2025Article
- An N-terminal acidic β-sheet domain is responsible for the metal-accumulation properties of amyloid-β protofibrils: a molecular dynamics study.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024Article
- Article
- MAD-microbial (origin of) Alzheimer's disease hypothesis: from infection and the antimicrobial response to disruption of key copper-based systems.Frontiers in neuroscience · 2024Review
- Copper binding and protein aggregation: a journey from the brain to the human lens.RSC chemical biology · 2023Article
- Probing the Structure of Toxic Amyloid-β Oligomers with Electron Spin Resonance and Molecular Modeling.ACS chemical neuroscience · 2021Article
- A label-free fluorescent peptide probe for sensitive and selective determination of copper and sulfide ions in aqueous systems.RSC advances · 2021Article
- Copper Dyshomeostasis in Neurodegenerative Diseases-Therapeutic Implications.International journal of molecular sciences · 2020Review
- Rhodamine-Based Metal Chelator: A Potent Inhibitor of Metal-Catalyzed Amyloid Toxicity.ACS omega · 2020Article
- IRF-8 is Involved in Amyloid-βJournal of molecular neuroscience : MN · 2017Article
- Amyloid scaffolds as alternative chlorosomes.Organic & biomolecular chemistry · 2017Review
- The Case for Abandoning Therapeutic Chelation of Copper Ions in Alzheimer's Disease.Frontiers in neuroscience · 2017Review
- Numerical Simulations Reveal Randomness of Cu(II) Induced Aβ Peptide Dimerization under Conditions Present in Glutamatergic Synapses.PloS one · 2017Article
- Orientation of tyrosine side chain in neurotoxic Aβ differs in two different secondary structures of the peptide.Royal Society open science · 2016Article
- High-resolution analytical imaging and electron holography of magnetite particles in amyloid cores of Alzheimer's disease.Scientific reports · 2016Article
- On the generation of OH(·) radical species from H2O2 by Cu(I) amyloid beta peptide model complexes: a DFT investigation.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Article
- PET Imaging of Copper Trafficking in a Mouse Model of Alzheimer Disease.Journal of nuclear medicine : official publication, Society of Nuclear Medicine · 2016Article
- Truncated Amyloid-β(11-40/42) from Alzheimer Disease Binds Cu2+ with a Femtomolar Affinity and Influences Fiber Assembly.The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Copper coexists with amyloid-β (Aβ) peptides at a high concentration in the senile plaques of Alzheimer's disease (AD) patients and has been linked to oxidative damage associated with AD pathology. However, the origin of copper and the driving force behind its accumulation are unknown. We designed a sensitive fluorescent probe, Aβ(1-16)(Y10W), by substituting the tyrosine residue at position 10 in the hydrophilic domain of Aβ(1-42) with tryptophan. Upon mixing Cu(II), Aβ(1-16)(Y10W), and aliquots of Aβ(1-42) taken from samples incubated for different lengths of time, we found that the Cu(II) binding strength of aggregated Aβ(1-42) has been elevated by more than 2 orders of magnitude with respect to that of monomeric Aβ(1-42). Electron paramagnetic spectroscopic measurements revealed that the Aβ(1-42) aggregates, unlike their monomeric form, can seize copper from human serum albumin, an abundant copper-containing protein in brain and cerebrospinal fluid. The significantly elevated binding strength of the Aβ(1-42) aggregates can be rationalized by a Cu(II) coordination sphere constituted by three histidines from two adjacent Aβ(1-42) molecules. Our work demonstrates that the copper binding affinity of Aβ(1-42) is dependent on its aggregation state and provides new insight into how and why senile plaques accumulate copper in vivo.
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