ArticleThe Journal of biological chemistry2014
Capturing a reactive state of amyloid aggregates: NMR-based characterization of copper-bound Alzheimer disease amyloid β-fibrils in a redox cycle.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 51 citations in OpenAlex.
- The Role of Genetic, Environmental, and Dietary Factors in Alzheimer's Disease: A Narrative Review.International journal of molecular sciences · 2025Review
- The role of redox-active iron, copper, manganese, and redox-inactive zinc in toxicity, oxidative stress, and human diseases.EXCLI journal · 2025Review
- Semax, a Copper Chelator Peptide, Decreases the Cu(II)-Catalyzed ROS Production and Cytotoxicity of aβ by Metal Ion Stripping and Redox Silencing.Bioinorganic chemistry and applications · 2025Article
- Exosomal Dynamics and Brain Redox Imbalance: Implications in Alzheimer's Disease Pathology and Diagnosis.Antioxidants (Basel, Switzerland) · 2024Review
- Pentoxifylline as Add-On Treatment to Donepezil in Copper Sulphate-Induced Alzheimer's Disease-Like Neurodegeneration in Rats.Neurotoxicity research · 2023Article
- The Influence of Copper Nanoparticles on Neurometabolism Marker Levels in the Brain and Intestine in a Rat Model.International journal of molecular sciences · 2023Article
- Complement System in Alzheimer's Disease.International journal of molecular sciences · 2021Review
- Copper Toxicity Links to Pathogenesis of Alzheimer's Disease and Therapeutics Approaches.International journal of molecular sciences · 2020Review
- Lipid-nanodiscs formed by paramagnetic metal chelated polymer for fast NMR data acquisition.Biochimica et biophysica acta. Biomembranes · 2020Article
- Structural Studies of Amyloid Fibrils by Paramagnetic Solid-State Nuclear Magnetic Resonance Spectroscopy.Journal of the American Chemical Society · 2018Article
- Implications of peptide assemblies in amyloid diseases.Chemical Society reviews · 2017Review
- Identification of key structural features of the elusive Cu-Aβ complex that generates ROS in Alzheimer's disease.Chemical science · 2017Article
- Vitamin C, Aging and Alzheimer's Disease.Nutrients · 2017Review
- The Influence of Cigarette Smoke Exposure on the Copper Concentration in the Serum Depending on the Use of Menopausal Hormone Therapy.BioMed research international · 2017Article
- Role of Copper in the Onset of Alzheimer's Disease Compared to Other Metals.Frontiers in aging neuroscience · 2017Review
- 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
- Reactivity of Metal-Free and Metal-Associated Amyloid-β with Glycosylated Polyphenols and Their Esterified Derivatives.Scientific reports · 2015Article
- Structural studies of proteins by paramagnetic solid-state NMR spectroscopy.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015Article
- In vitro effect of H2O 2, some transition metals and hydroxyl radical produced via fenton and fenton-like reactions, on the catalytic activity of AChE and the hydrolysis of ACh.Neurochemical research · 2014Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The interaction of redox-active copper ions with misfolded amyloid β (Aβ) is linked to production of reactive oxygen species (ROS), which has been associated with oxidative stress and neuronal damages in Alzheimer disease. Despite intensive studies, it is still not conclusive how the interaction of Cu(+)/Cu(2+) with Aβ aggregates leads to ROS production even at the in vitro level. In this study, we examined the interaction between Cu(+)/Cu(2+) and Aβ fibrils by solid-state NMR (SSNMR) and other spectroscopic methods. Our photometric studies confirmed the production of ~60 μM hydrogen peroxide (H2O2) from a solution of 20 μM Cu(2+) ions in complex with Aβ(1-40) in fibrils ([Cu(2+)]/[Aβ] = 0.4) within 2 h of incubation after addition of biological reducing agent ascorbate at the physiological concentration (~1 mM). Furthermore, SSNMR (1)H T1 measurements demonstrated that during ROS production the conversion of paramagnetic Cu(2+) into diamagnetic Cu(+) occurs while the reactive Cu(+) ions remain bound to the amyloid fibrils. The results also suggest that O2 is required for rapid recycling of Cu(+) bound to Aβ back to Cu(2+), which allows for continuous production of H2O2. Both (13)C and (15)N SSNMR results show that Cu(+) coordinates to Aβ(1-40) fibrils primarily through the side chain Nδ of both His-13 and His-14, suggesting major rearrangements from the Cu(2+) coordination via Nε in the redox cycle. (13)C SSNMR chemical shift analysis suggests that the overall Aβ conformations are largely unaffected by Cu(+) binding. These results present crucial site-specific evidence of how the full-length Aβ in amyloid fibrils offers catalytic Cu(+) centers.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.