Metal catalyzed oxidation of tyrosine residues by different oxidation systems of copper/hydrogen peroxide

Ali, Feda E.; Barnham, Kevin J.; Barrow, Colin J.; Separovic, Frances

doi:10.1016/j.jinorgbio.2003.10.002

Cited by 55 publications

(39 citation statements)

References 60 publications

(66 reference statements)

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“…In addition to Ab methionine sulfoxide, Ab may also be oxidatively modified by the addition of other adducts including aldehyde adducts to the lysine residues [88] and tyrosine modified with adducts such as DOPA, dopamine, dopamine quinine, dihydroxyindol and isodityrosine [89]. Ab extracted from AD plaques contains oxidative modifications such as oxidised Met 35 [85,87], modification of the histidine residues to 2-oxo-histidine [90] and oxidatively modified tyrosine adducts including 3,4-dihydroxyphenylalanine (DOPA), dopamine and dopamine quinine [90,91].…”

Section: Ab Redox Chemistrymentioning

confidence: 99%

Delineating the Mechanism of Alzheimer’s Disease Aβ Peptide Neurotoxicity

2007

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The Alzheimer's disease neurotoxic amyloid-beta (A beta) peptide is derived from the larger amyloid precursor protein (APP) and is the principal component of the senile plaques in Alzheimer's disease (AD) brains. This mechanism by which A beta mediates neurotoxicity or neuronal dysfunction is not fully resolved. This review will outline some of the key determinants that modulate A beta's activity and the cellular pathways and mechanisms involved.

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Section: Ab Redox Chemistrymentioning

confidence: 99%

Delineating the Mechanism of Alzheimer’s Disease Aβ Peptide Neurotoxicity

2007

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“…9(C)] residues. The linkage was attributed to Tyr residue since it is known that Tyr forms Tyr-Tyr cross-links (Orhan et al, 2005;Giulivi et al, 2003;Ali et al, 2004).…”

Section: + the Fragmentation Of The [M + H]mentioning

confidence: 99%

“…• generation via one-electron reduction are Fe(II) (under Fenton's reaction conditions; Stadtman and Berlett, 1991;Berlett and Stadtman, 1997;Stadtman and Levine, 2003), Cu (I) (Berlett and Stadtman, 1997) and Cu (II) (Ali et al, 2004). Oxidation reactions can induce modification on amino acid side chains, by generating intact proteins with additional oxygens, promoting cleavage of protein backbone and/or protein-protein cross-linkages (Berlett and Stadtman, 1997;Stadtman and Levine, 2003;Headlam and Davies, 2004).…”

Section: Introductionmentioning

confidence: 99%

Identification of leucine‐enkephalin radical oxidation products by liquid chromatography tandem mass spectrometry

Fonseca

Domingues

Reis

et al. 2008

Biomedical Chromatography

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The oxidation of the peptide leucine-enkephalin (YGGFL) induced by the hydroxyl radical (HO*), formed under Fenton-like conditions [Cu (II)/H(2)O(2)], was studied and monitored by LC-MS. The oxidation products identified included products resultant from (a) the insertion of oxygen atoms (1-5), (b) peptide backbone cleavage (short-chain products formed by diamide pathway) and (c) radical-radical crosslinking reactions. In order to identify the modified residues, LC-MS/MS spectra were obtained. The insertion of oxygen atoms into the peptide originated hydroxide, di-hydroxide and/or hydroperoxide derivatives. In addition it was found that the aromatic amino acids are most susceptible to being hydroxylated, while the aliphatic amino acids are more prone to forming hydroperoxides. Oxidation products with double bonds were also identified. The short chain products resulted from the alpha-carbon radical of terminal amino acids (Tyr and Leu). Products resulting from cross-linking reactions between intact carbon-centered peptide radical (with and without one HO group) and a side chain radical (*C(7)H(7)O) were identified. It was found that, although all amino acids residues of the peptide undergo modifications, the N-terminal seems to be prone to oxidative modifications under these conditions.

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“…Abundance of redox active transition metal ions like iron in the brain makes it more susceptible to oxidative stress via the metal-catalysed formation of reactive oxygen species (ROS) (Ali, Barnham, Barrow, & Separovic, 2004). In addition, brain regions show differential sensitivity to oxidative stress because of the differential antioxidant profile, involving antioxidant enzymes and endogenous antioxidants like glutathione and vitamin E (Lieber, 2005;.…”

Section: Introductionmentioning

confidence: 99%