Products of Cu(II)-catalyzed oxidation in the presence of hydrogen peroxide of the 1–10, 1–16 fragments of human and mouse β-amyloid peptide
Abstract
The interactions of proteins with reactive oxygen species (ROS) may result in covalent modifications of amino acid residues in proteins, formation of protein-protein cross-linkages, and oxidation of the protein backbone resulting in protein fragmentation. In an attempt to elucidate the products of the metal-catalyzed oxidation of the human (H) and mouse (M) (1-10H), (1-10M), (1-16H) and (1-16M) fragments of beta-amyloid peptide, the high performance liquid chromatography (HPLC) and matrix-assisted laser desorption/ionization mass spectrometry (MALDI-TOF MS) methods and Cu(II)/H(2)O(2) as a model oxidizing system were employed. Peptide solution (0.50 mM) was incubated at 37 degrees C for 24 h with metal:peptide:H(2)O(2) molar ratio 1:1:1 for the (1-16H), (1-16M) fragments, and 1:1:2 for the (1-10H), (1-10M) peptides in phosphate buffer, pH 7.4. Oxidation targets for all peptide studied are the histidine residues coordinated to the metal ions. For the (1-16H) peptide are likely His(13) and/or His(14), and for the (1-16M) fragment His(6) and/or His(14), which are converted to 2-oxo-His. Metal-binding residue, the aspartic acid (D(1)) undergoes the oxidative decarboxylation and deamination to pyruvate. The cleavages of the peptide bonds by either the diamide or alpha-amidation pathways were also observed.
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Both in vitro and in vivo studies pointed out the Aβ peptide as a target molecule of metal-catalyzed oxidation.
“Moreover, both in vitro and in vivo studies pointed out the Aβ peptide as a target molecule of metal-catalyzed oxidation (Näslund et al., 1994; Kowalik-Jankowska et al., 2004; Inoue et al., 2009).”
From Exploring the Therapeutic Potential of Phytochemicals in Alzheimer’s Disease: Focus on Polyphenols and Monoterpenes (2022) · cites this paper as Kowalik-Jankowska et al., 2004
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- Authors
- Kowalik-Jankowska, T., Ruta, M., Wiśniewska, K., Łankiewicz, L., & Dyba, M.
- Affiliations
- University of Wrocław (PL)
- University of Gdańsk (PL)
- Venue
- Journal of Inorganic Biochemistry
- Publisher
- Elsevier BV
- Published
- 2004-06
- Volume
- 98
- Issue
- 6
- Pages
- 940-950
- ISSN
- 0162-0134 (ISSN-L)
- OpenAlex
- W2096297439
- Cited by
- 92
- References
- 60
- Citations by year
- 2026: 2 · 2025: 5 · 2024: 2 · 2023: 3 · 2022: 3 · 2021: 2 · 2020: 5 · 2019: 7 · 2017: 5 · 2016: 9 · 2015: 3 · 2014: 3 · 2013: 3 · 2012: 6
- FWCI
- 3.50
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Inorganic Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- beta-amyloid peptide, hydrogen peroxide, protein oxidation, histidine oxidation, oxidative decarboxylation, peptide bond cleavage, alpha-amidation, reactive oxygen species
- MeSH terms
- Animals, Catalysis, Copper, Humans, Hydrogen Peroxide, Oxidation-Reduction, Peptides, Amyloid beta-Peptides, Mice
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