ParkinsonCanadaV1, Main, Exploration, bibRecord, 001161

Oxidative Stress Effect of Dopamine on α-Synuclein: Electroanalysis of Solvent Interactions

Identifieur interne : 001161 ( Main/Exploration ); précédent : 001160; suivant : 001162

Oxidative Stress Effect of Dopamine on α-Synuclein: Electroanalysis of Solvent Interactions

Auteurs : Tiffiny Chan ; Ari M. Chow ; Xin R. Cheng ; Derek X0a W. F. Tang ; Ian R. Brown ; Kagan Kerman

Source :

ACS Chemical Neuroscience [ 1948-7193 ] ; 2012.

RBID : PMC:3399574

Abstract

The interaction of dopamine (DA) and α-synuclein (α-S) can lead to protein misfolding and neuronal death triggered by oxidative stress relevant to the progression of Parkinson’s disease (PD). In this study, interfacial properties associated with DA-induced α-S aggregation under various solution conditions (i.e., pH, ionic strength) were investigated in vitro. The electrochemical oxidation of tyrosine (Tyr) residues in α-S was detected in the presence of DA. DA concentration dependence was analyzed and found to significantly affect α-S aggregation pathways. At low pH, DA was shown to be stable and produced no observable difference in interfacial properties. Between pH 7 and 11, DA promoted α-S aggregation. Significant differences in oxidation current signals in response to high pH and ionic strength suggested the importance of initial interactions in the stabilization of toxic oligomeric structures and subsequent off-pathways of α-S. Our results demonstrate the importance of solution interactions with α-S and the unique information that electrochemical techniques can provide for the investigation of α-S aggregation at early stages, an important step toward the development of future PD therapeutics.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3399574

DOI: 10.1021/cn300034t
PubMed: 22860226
PubMed Central: 3399574

Affiliations:

Le document en format XML

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<p>The interaction of dopamine (DA) and α-synuclein
(α-S)
can lead to protein misfolding and neuronal death triggered by oxidative
stress relevant to the progression of Parkinson’s disease (PD).
In this study, interfacial properties associated with DA-induced α-S
aggregation under various solution conditions (i.e., pH, ionic strength)
were investigated in vitro. The electrochemical oxidation of tyrosine
(Tyr) residues in α-S was detected in the presence of DA. DA
concentration dependence was analyzed and found to significantly affect
α-S aggregation pathways. At low pH, DA was shown to be stable
and produced no observable difference in interfacial properties. Between
pH 7 and 11, DA promoted α-S aggregation. Significant differences
in oxidation current signals in response to high pH and ionic strength
suggested the importance of initial interactions in the stabilization
of toxic oligomeric structures and subsequent off-pathways of α-S.
Our results demonstrate the importance of solution interactions with
α-S and the unique information that electrochemical techniques
can provide for the investigation of α-S aggregation at early
stages, an important step toward the development of future PD therapeutics.</p>
</div>
</front>
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<name sortKey="Cheng, Xin R" sort="Cheng, Xin R" uniqKey="Cheng X" first="Xin R." last="Cheng">Xin R. Cheng</name>
<name sortKey="Chow, Ari M" sort="Chow, Ari M" uniqKey="Chow A" first="Ari M." last="Chow">Ari M. Chow</name>
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<name sortKey="Tang, Derek X0a W F" sort="Tang, Derek X0a W F" uniqKey="Tang D" first="Derek X0a W. F." last="Tang">Derek X0a W. F. Tang</name>
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La maladie de Parkinson au Canada (serveur d'exploration)

Oxidative Stress Effect of Dopamine on α-Synuclein: Electroanalysis of Solvent Interactions

Oxidative Stress Effect of Dopamine on α-Synuclein: Electroanalysis of Solvent Interactions

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Abstract

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