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Products of Cu(II)-catalyzed oxidation in the presence of hydrogen peroxide of the 1-10, 1-16 fragments of human and mouse beta-amyloid peptide.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Kowalik-Jankowska, Teresa Ruta, Monika Wiśniewska, Kornelia Łankiewicz, Leszek Dyba, Marcin |
| Copyright Year | 2004 |
| 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. |
| File Format | PDF HTM / HTML |
| DOI | 10.1016/j.jinorgbio.2004.03.001 |
| PubMed reference number | 15149800 |
| Journal | Medline |
| Volume Number | 98 |
| Issue Number | 6 |
| Alternate Webpage(s) | http://marcindyba.com/wp-content/uploads/publications/M_Dyba-J_Inorg_Biochem_2004_98_6_940-950.pdf |
| Alternate Webpage(s) | https://doi.org/10.1016/j.jinorgbio.2004.03.001 |
| Journal | Journal of inorganic biochemistry |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
