期刊
MOLECULES
卷 25, 期 4, 页码 -出版社
MDPI
DOI: 10.3390/molecules25040961
关键词
peroxymonocarbonate; carbonate radical anion; beta-amyloid; methionine sulfoxide; sulfur centered radical; reactive sulfur species; sulfur radical cation
资金
- Sapienza Ateneo 2019 Avvio alla Ricerca (Sapienza University of Rome)
- EMBO
The beta-amyloid (A beta) peptide plays a key role in the pathogenesis of Alzheimer's disease. The methionine (Met) residue at position 35 in A beta C-terminal domain is critical for neurotoxicity, aggregation, and free radical formation initiated by the peptide. The role of Met in modulating toxicological properties of A beta most likely involves an oxidative event at the sulfur atom. We therefore investigated the one- or two-electron oxidation of the Met residue of A beta(25-35) fragment and the effect of such oxidation on the behavior of the peptide. Bicarbonate promotes two-electron oxidations mediated by hydrogen peroxide after generation of peroxymonocarbonate (HCO4-, PMC). The bicarbonate/carbon dioxide pair stimulates one-electron oxidations mediated by carbonate radical anion (CO3 center dot-). PMC efficiently oxidizes thioether sulfur of the Met residue to sulfoxide. Interestingly, such oxidation hampers the tendency of A beta to aggregate. Conversely, CO3 center dot- causes the one-electron oxidation of methionine residue to sulfur radical cation (MetS(center dot+)). The formation of this transient reactive intermediate during A beta oxidation may play an important role in the process underlying amyloid neurotoxicity and free radical generation.
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