Products of Cu(II)-catalyzed oxidation of the N-terminal fragments of α-synuclein in the presence of hydrogen peroxide

Kowalik-Jankowska, Teresa; Rajewska, A.; Jankowska, Elżbieta; Wiśniewska, Kornelia; Grzonka, Zbigniew

doi:10.1016/j.jinorgbio.2006.05.010

Cited by 36 publications

(25 citation statements)

References 61 publications

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“…This observation supports previous reports that methionine sulfone oxidation is substantially enhanced when the side chain is in close proximity to a metal ion containing group in what is referred to as a caged process (7,30,31). The presence of sulfones at the Met-67 position in the HbF variant supports this view because the thiol ether side chain is clearly very close to the reactive heme iron atom as shown in the crystal structure (see below).…”

Section: Oxidation Reactions At the E11 Position In The ␥ Fetal Hb Susupporting

confidence: 91%

Post-translational Transformation of Methionine to Aspartate Is Catalyzed by Heme Iron and Driven by Peroxide

Strader

Hicks

Kassa

et al. 2014

Journal of Biological Chemistry

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Section: Oxidation Reactions At the E11 Position In The ␥ Fetal Hb Susupporting

confidence: 91%

Post-translational Transformation of Methionine to Aspartate Is Catalyzed by Heme Iron and Driven by Peroxide

Strader

Hicks

Kassa

et al. 2014

Journal of Biological Chemistry

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“…Affinity data for Cu II forA ba nd aS have been measured under different conditions and by different groups.D ifferent values wereo btained depending on the conditions, and this have been reviewed recently. [4,[29][30][31][32] Complete measurements under the same conditions and by the same group wereo btained for truncatedA ba nd aS by potentiometry.T he reported dissociation constants for Ab1-16 and aS1-17a tp H7.4 in the absence of buffer are 0.207 [42] and 0.94 nm, [12] respectively.T he peptide MD-aS31-56, which mimics binding of Cu II to aS including His50, has a K d value of 0.19 nm. [35] Ab1-16h as aC u II affinity about five times highert han that of aS at pH 7.4 (when only the N-terminal site is occupied), but as imilar affinity when His50 is also involved in the Cu II binding.…”

Section: Resultsmentioning

confidence: 97%

“…aS (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15) and bS(1-15) lyophilised peptides were weighed and dissolved in pure water to provide three high-concentration stock solutions. The stock solution concentrations of both aS (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15) and ChemBioChem 2015ChemBioChem , 16,2319ChemBioChem -2328 www.chembiochem.org bS (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15) were titrated by UV/Vis absorption with monitoring of the phenylalanine absorption peak at 258 nm (typical of Phe-containing peptides), with am olar extinction coefficient of 195 m À1 cm À1 ,r esulting in 1.80 mm and 2.57 mm stock solutions for aS (1)…”

Section: Methodsmentioning

confidence: 99%

“…Cu-Ab and Cu-aS are able to catalysethe productiono fROS in the presence of aphysiological reducing agent (e.g.,a scorbate) and dioxygen, ar eaction proposed to contribute to neurodegeneration. [11][12][13] Thus it was proposed that in AD and PD copperi sm isplaced, rathert han ab ulk overloado rb ulk deficiency such as in Wilson's or Menkes diseases. [14] Ab and aS form amyloid-type aggregates under disease conditions througha na utocatalytic self-assembly mechanism.…”

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confidence: 99%

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Copper(I/II), α/β‐Synuclein and Amyloid‐β: Menage à Trois?

et al. 2015

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Copper binding to α-synuclein (aS) and to amyloid-β (Ab) has been connected to Parkinson's and Alzheimer's disease (AD), respectively, because Cu ions can modulate the peptide aggregation, and these Cu ⋅ peptide complexes can catalyse the production of reactive oxygen species (ROS). In a significant proportion of AD brains, aggregation of aS and Ab has been detected, and it was proposed that Ab and aS interact with each other. Thus, we investigated the potential interactions of Ab and aS through their binding of copper(I) and copper(II). Additionally, β-synuclein (bS) was investigated, due to its additional methionine residue, a potential Cu(I) ligand. We found that: 1) the peptides containing the Cu-binding domains Ab1-16, aS1-15 and bS1-15 have similar affinities towards Cu(II) and towards Cu(I), with Ab1-16 being slightly stronger, 2) in the case of Cu(I), the additional Met residue in bS1-15 increased the affinity slightly, 3) the exchange of Cu(I/II) between the two peptides is rapid (≤ ms), 4) a/bS1-15 and Ab1-16 form a heterodimeric complex with Cu(II), 5) Cu(I) probably promotes a transient ternary complex, 6) the different Cu(I/II) coordination of Ab1-16, aS1-15 and bS1-15 impacts the capacity to produce ROS and to oxidise catechol, and 7) when Ab1-16, aS1-15 and Cu are present, the ROS production more closely resembles that by Ab1-16. The work gives insights into the coordination chemistry of these related peptides, and the relevance of coordination differences, the ternary complex and ROS production are discussed.

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“…They showed that aspartate in the first 17 amino acid residues plays an important role in the co‐ordination of Cu [61]. This interaction can also result in the oxidation of methionine residues [62]. However, using similar techniques, the same group showed that Cu is co‐ordinated with a peptide with residues 39–56 and that both the histidine and lysine residues are involved in the co‐ordination [63].…”

Section: Metal Bindingmentioning

confidence: 99%

Interactions between metals and α‐synuclein − function or artefact?

Brown

2007

The FEBS Journal

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α‐synuclein is one of a family of proteins whose function remains unknown. This protein has become linked to a number of neurodegenerative disease although its potential causative role in these diseases remains mysterious. In diseases such as Parkinson's disease and Lewy body dementias, α‐synuclein becomes deposited in aggregates termed Lewy bodies. Also, some inherited forms of Parkinson's diseases are linked to mutations in the gene for α‐synuclein. Studies have mostly focussed on what causes the aggregation of the protein but, like many amyloidogenic proteins associated with a neurodegenerative disorder, this protein has now been suggested to bind copper. This finding is currently controversial. This review examines the evidence that α‐synuclein is a copper binding protein and discusses whether this has any significance in determining the function of the protein or whether copper binding is at all necessary for aggregation.

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Products of Cu(II)-catalyzed oxidation of the N-terminal fragments of α-synuclein in the presence of hydrogen peroxide

Cited by 36 publications

References 61 publications

Post-translational Transformation of Methionine to Aspartate Is Catalyzed by Heme Iron and Driven by Peroxide

Post-translational Transformation of Methionine to Aspartate Is Catalyzed by Heme Iron and Driven by Peroxide

Copper(I/II), α/β‐Synuclein and Amyloid‐β: Menage à Trois?

Interactions between metals and α‐synuclein − function or artefact?

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