ArticleBiomolecules2019
Mercury and Alzheimer's Disease: Hg(II) Ions Display Specific Binding to the Amyloid-β Peptide and Hinder Its Fibrillization.
Article in Biomolecules, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Tracing the threads: How toxic metals contribute to neurodegeneration.IBRO neuroscience reports · 2026Review
- Binding of Hg(I) and Hg(II) Ions to Amyloid-Beta (Aβ) Peptide Variants Affect their Structure and Aggregation.Chembiochem : a European journal of chemical biology · 2025Article
- Molecular interactions, structural effects, and binding affinities between silver ions (AgScientific reports · 2025Article
- Peptide-Based Rapid and Selective Detection of Mercury in Aqueous Samples with Micro-Volume Glass Capillary Fluorometer.Biosensors · 2024Article
- Environmental Toxins and Alzheimer's Disease: a Comprehensive Analysis of Pathogenic Mechanisms and Therapeutic Modulation.Molecular neurobiology · 2024Review
- Characterization of Uranyl (UOACS chemical neuroscience · 2023Article
- Residue-specific binding of Ni(II) ions influences the structure and aggregation of amyloid beta (Aβ) peptides.Scientific reports · 2023Article
- Zebrafish as a Potential Model for Neurodegenerative Diseases: A Focus on Toxic Metals Implications.International journal of molecular sciences · 2023Review
- Mercury Ion Binding to Apolipoprotein E Variants ApoE2, ApoE3, and ApoE4: Similar Binding Affinities but Different Structure Induction Effects.ACS omega · 2022Article
- Comprehensive Review Regarding Mercury Poisoning and Its Complex Involvement in Alzheimer's Disease.International journal of molecular sciences · 2022Review
- Parkinson's Disease and the Metal-Microbiome-Gut-Brain Axis: A Systems Toxicology Approach.Antioxidants (Basel, Switzerland) · 2021Review
- Metals in ALS TDP-43 Pathology.International journal of molecular sciences · 2021Review
- An Overview of Several Inhibitors for Alzheimer's Disease: Characterization and Failure.International journal of molecular sciences · 2021Review
- Toxic Environmental Factors and their Association with the Development of Dementia: a Mini Review on Heavy Metals and Ambient Particulate Matter.Materia socio-medica · 2020Review
- Aluminium Binding to Modified Amyloid-β Peptides: Implications for Alzheimer's Disease.Molecules (Basel, Switzerland) · 2020Article
- Metal ion coordination delays amyloid-β peptide self-assembly by forming an aggregation-inert complex.The Journal of biological chemistry · 2020Article
- Hormetic-Like Effects of L-Homocysteine on Synaptic Structure, Function, and Aβ Aggregation.Pharmaceuticals (Basel, Switzerland) · 2020Article
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Brains and blood of Alzheimer's disease (AD) patients have shown elevated mercury concentrations, but potential involvement of mercury exposure in AD pathogenesis has not been studied at the molecular level. The pathological hallmark of AD brains is deposition of amyloid plaques, consisting mainly of amyloid-β (Aβ) peptides aggregated into amyloid fibrils. Aβ peptide fibrillization is known to be modulated by metal ions such as Cu(II) and Zn(II). Here, we study in vitro the interactions between Aβ peptides and Hg(II) ions by multiple biophysical techniques. Fluorescence spectroscopy and atomic force microscopy (AFM) show that Hg(II) ions have a concentration-dependent inhibiting effect on Aβ fibrillization: at a 1:1 Aβ·Hg(II) ratio only non-fibrillar Aβ aggregates are formed. NMR spectroscopy shows that Hg(II) ions interact with the N-terminal region of Aβ(1-40) with a micromolar affinity, likely via a binding mode similar to that for Cu(II) and Zn(II) ions, i.e., mainly via the histidine residues His6, His13, and His14. Thus, together with Cu(II), Fe(II), Mn(II), Pb(IV), and Zn(II) ions, Hg(II) belongs to a family of metal ions that display residue-specific binding interactions with Aβ peptides and modulate their aggregation processes.
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