On the generation of OH(.) radical species from H2O2 by Cu(I) amyloid beta peptide model complexes: A DFT investigation
Abstract
According to different studies, the interaction between amyloid β-peptide (Aβ) and copper ions could yield radical oxygen species production, in particular the highly toxic hydroxyl radical OH(·) that is suspected to contribute to Alzheimer's disease pathogenesis. Despite intensive experimental and computational studies, the nature of the interaction between copper and Aβ peptide, as well as the redox reactivity of the system, are still matter of debate. It was proposed that in Cu(II) → Cu(I) reduction the complex Cu(II)-Aβ could follow a multi-step conformational change with redox active intermediates that may be responsible for OH(·) radical production from H2O2 through a Fenton-like process. The purpose of this work is to evaluate, using ab initio Density Functional Theory computations, the reactivity of different Cu(I)-Aβ coordination modes proposed in the literature, in terms of OH(·) production. For each coordination model, we considered the corresponding H2O2 adduct and performed a potential energy surface scan along the reaction coordinate of O-O bond dissociation of the peroxide, resulting in the production of OH(·) radical, obtaining reaction profiles for the evaluation of the energetic of the process. This procedure allowed us to confirm the hypothesis according to which the most populated Cu(I)-Aβ two-histidine coordination is not able to perform efficiently H2O2 reduction, while a less populated three-coordinated form would be responsible for the OH(·) production. We show that coordination modes featuring a third nitrogen containing electron-donor ligand (an imidazole ring of an histidine residue is slightly favored over the N-terminal amine group) are more active towards H2O2 reduction.
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In the reaction between Aβ and Cu, H2O2 and ROS increase, evidencing a key role of H2O2 in the development of Alzheimer's disease pathology.
“In this reaction, H2O2 and the increase in ROS are linked, thus evidencing the key role of the H2O2 molecule in the development of AD pathology [125].”
From Multi-Target Mechanisms of Phytochemicals in Alzheimer’s Disease: Effects on Oxidative Stress, Neuroinflammation and Protein Aggregation (2022) · cites this paper as [125]
Aβ peptides have a high affinity for Cu ions, producing a 1:1 complex, which favors aggregation and formation of amyloid plaques.
“Peptides (Aβ) have a high affinity for Cu ions, producing a 1:1 complex, which favors the aggregation and formation of amyloid plaques.”
From Multi-Target Mechanisms of Phytochemicals in Alzheimer’s Disease: Effects on Oxidative Stress, Neuroinflammation and Protein Aggregation (2022) · cites this paper as [125]
In Alzheimer's disease, excessive oxidative stress manifests from the early stages of the disease.
“Particularly for AD, excessive OS manifests itself from the early stages of the disease [72,125].”
From Multi-Target Mechanisms of Phytochemicals in Alzheimer’s Disease: Effects on Oxidative Stress, Neuroinflammation and Protein Aggregation (2022) · cites this paper as [125]
A link exists between increases in ROS, H2O2, metal ions, and the Aβ peptide.
“the existence of a link between the increase in ROS, H2O2, metal ions, and the peptide Aβ [125] has been suggested.”
From Multi-Target Mechanisms of Phytochemicals in Alzheimer’s Disease: Effects on Oxidative Stress, Neuroinflammation and Protein Aggregation (2022) · cites this paper as [125]
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- Authors
- Prosdocimi, T., De Gioia, L., Zampella, G., & Bertini, L.
- Affiliations
- University of Milano-Bicocca (IT)
- Corresponding author
- Bertini, Luca
- Venue
- JBIC Journal of Biological Inorganic Chemistry
- Published
- 2015-12-28
- Volume
- 21
- Issue
- 2
- Pages
- 197-212
- ISSN
- 0949-8257 (ISSN-L)
- 1432-1327
- OpenAlex
- W2208747957
- Cited by
- 32
- References
- 57
- Citations by year
- 2025: 1 · 2024: 3 · 2023: 5 · 2022: 3 · 2021: 3 · 2020: 3 · 2019: 4 · 2018: 3 · 2017: 7
- FWCI
- 2.46
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- JBIC Journal of Biological Inorganic Chemistry (publishedVersion)
- PubMed (publishedVersion)
- BOA (University of Milano-Bicocca) (submittedVersion)
- Funders
- Ministero dell'Istruzione, dell'Università e della Ricerca (PRIN 2010M2ARJ_010)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Physical Sciences › Chemistry › Organic Chemistry › Free Radicals and Antioxidants
- Keywords
- amyloid-beta, copper(I) complexes, hydroxyl radical generation, hydrogen peroxide reduction, Fenton-like reaction, Alzheimer's disease, coordination modes, histidine coordination, imidazole ligands, potential energy surface, O-O bond dissociation
- MeSH terms
- Copper, Hydrogen Peroxide, Models, Chemical, Peptide Fragments, Amyloid beta-Peptides, Hydroxyl Radical
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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