Dual roles of tau R peptides on Cu(II)/(I)-mediated reactive oxygen species formation

Golec, Camilla; Mortensen, Shaelyn; Anwar, Saba; Martic-Milne, Sanela

doi:10.1007/s00775-021-01902-7

Cited by 4 publications

(1 citation statement)

References 37 publications

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“…It was also confirmed that during the reaction, Cu(II) ions are reduced to Cu(I) ions and both peptides (L1 and L2) tend to aggregate [58]. Moreover, the L2 ligand is responsible for filament formation after the addition of the metal ion and ascorbic acid (reducing agent) [59]. The obtained results show that metal ion chelation by peptides derived from the Tau protein may influence the initiation of Alzheimer's disease.…”

Section: Neurodegenerative Disorders 211 Tau (T) Proteinmentioning

confidence: 59%

The Bright and Dark Sides of Reactive Oxygen Species Generated by Copper–Peptide Complexes

et al. 2022

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Copper ions bind to biomolecules (e.g., peptides and proteins) playing an essential role in many biological and physiological pathways in the human body. The resulting complexes may contribute to the initiation of neurodegenerative diseases, cancer, and bacterial and viral diseases, or act as therapeutics. Some compounds can chemically damage biological macromolecules and initiate the development of pathogenic states. Conversely, a number of these compounds may have antibacterial, antiviral, and even anticancer properties. One of the most significant current discussions in Cu biochemistry relates to the mechanisms of the positive and negative actions of Cu ions based on the generation of reactive oxygen species, including radicals that can interact with DNA molecules. This review aims to analyze various peptide–copper complexes and the mechanism of their action.

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Section: Neurodegenerative Disorders 211 Tau (T) Proteinmentioning

confidence: 59%

The Bright and Dark Sides of Reactive Oxygen Species Generated by Copper–Peptide Complexes

et al. 2022

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Intercommunication between metal ions and amyloidogenic peptides or proteins in protein misfolding disorders

Suh

Kim

Yoo

et al. 2023

Coordination Chemistry Reviews

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Interactions of Copper(II) and Zinc(II) Ions with the Peptide Fragments of Proteins Related to Neurodegenerative Disorders: Similarities and Differences

Sóvágó

Várnagy

Kállay

et al. 2023

CMC

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Metal binding ability and coordination modes of the copper(II) and zinc(II) complexes of various peptide fragments of prion, amyloid-β and tau proteins are summarized in this review. Imidazole-N donors are the primary metal binding sites of all three proteins but the difference in the location of these residues and the presence or absence of other coordinating side chains results in significant differences in the complex formation processes. The presence of macrochelates and the possibility of the formation of multi-copper complexes is the most characteristic for prion fragments. Amyloid-β can form high stability complexes with both copper(II) and zinc(II) ions but the preferred binding sites are different for the two metal ions. Similar observations are obtained for the tau fragments but the metal ion selectivity of the various fragments is even more pronounced. In addition to the complex formation, copper(II) ions can play an important role in the various oxidative reactions of peptides. Results of the metal ion catalyzed oxidation of peptide fragments of prion, amyloid-β and tau proteins are also summarized. Amino acid side chain oxidation (mostly methionine, histidine and aspartic acid) and protein fragmentations are the most common consequences of this process.

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Dual roles of tau R peptides on Cu(II)/(I)-mediated reactive oxygen species formation

Cited by 4 publications

References 37 publications

The Bright and Dark Sides of Reactive Oxygen Species Generated by Copper–Peptide Complexes

The Bright and Dark Sides of Reactive Oxygen Species Generated by Copper–Peptide Complexes

Intercommunication between metal ions and amyloidogenic peptides or proteins in protein misfolding disorders

Interactions of Copper(II) and Zinc(II) Ions with the Peptide Fragments of Proteins Related to Neurodegenerative Disorders: Similarities and Differences

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