ParkinsonCanadaV1, PascalFrancis, Checkpoint, bibRecord, 000339

Interaction of baicalein and copper with α-synuclein: Electrochemical approach to Parkinson's Disease

Identifieur interne : 000339 ( PascalFrancis/Checkpoint ); précédent : 000338; suivant : 000340

Interaction of baicalein and copper with α-synuclein: Electrochemical approach to Parkinson's Disease

Auteurs : Tiffiny Chan [Canada] ; Arim. Chow [Canada] ; Derekw. F. Tang [Canada] ; QI LI [Canada] ; XUANYUANWANG [Canada] ; Ian R. Brown [Canada] ; Kagan Kerman [Canada]

Source :

Journal of electroanalytical chemistry : (1992) [ 1572-6657 ] ; 2010.

RBID : Pascal:11-0156674

Descripteurs français

Pascal (Inist)
- Baicaléine, Cuivre, Alpha-synucléine, Maladie de Parkinson, Agrégation, Voltammétrie cyclique, Onde carrée, Effet milieu, Méthode électrochimique, Interaction moléculaire, Dérivé de la flavone, Protéine.
Wicri :
- topic : Cuivre.

English descriptors

KwdEn :
- Aggregation, Alpha-synuclein, Baicalein, Copper, Cyclic voltammetry, Electrochemical method, Flavone derivatives, Medium effect, Molecular interaction, Parkinson disease, Protein, Square wave.

Abstract

Parkinson's Disease (PD) is a neurological disorder increasingly affecting the aging population worldwide. The presence of Lewy bodies is the cause of PD, where fibrillar α-synuclein is the major component. This report describes the electrochemical analysis of α-synuclein protein in the presence of factors that accelerate or inhibit the rate of its aggregation. Baicalein is an electro-active flavonoid that can act as a metal-chelator and form several products including quinones upon oxidation. Exposure to Cu(II) ions is known to cause significant acceleration in the rate of α-synuclein fibril formation. Square-wave voltammetry (SWV) of α-synuclein in the presence of these electro-active factors revealed distinct interfacial changes attributed to complex formation of α-synuclein with these species in vitro. The role of baicalein as a fibrillogenesis inhibitor was found to be most effective during the early stages of the fibril formation. The proof-of-principal results indicate that electrochemistry as a drug screening technique can provide a powerful tool for the discovery of new fibrillogenesis inhibitors as promising therapeutics for neurodegenerative diseases.

Affiliations:

Canada

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Le document en format XML

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<front><div type="abstract" xml:lang="en">Parkinson's Disease (PD) is a neurological disorder increasingly affecting the aging population worldwide. The presence of Lewy bodies is the cause of PD, where fibrillar α-synuclein is the major component. This report describes the electrochemical analysis of α-synuclein protein in the presence of factors that accelerate or inhibit the rate of its aggregation. Baicalein is an electro-active flavonoid that can act as a metal-chelator and form several products including quinones upon oxidation. Exposure to Cu(II) ions is known to cause significant acceleration in the rate of α-synuclein fibril formation. Square-wave voltammetry (SWV) of α-synuclein in the presence of these electro-active factors revealed distinct interfacial changes attributed to complex formation of α-synuclein with these species in vitro. The role of baicalein as a fibrillogenesis inhibitor was found to be most effective during the early stages of the fibril formation. The proof-of-principal results indicate that electrochemistry as a drug screening technique can provide a powerful tool for the discovery of new fibrillogenesis inhibitors as promising therapeutics for neurodegenerative diseases.</div>
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<fC01 i1="01" l="ENG"><s0>Parkinson's Disease (PD) is a neurological disorder increasingly affecting the aging population worldwide. The presence of Lewy bodies is the cause of PD, where fibrillar α-synuclein is the major component. This report describes the electrochemical analysis of α-synuclein protein in the presence of factors that accelerate or inhibit the rate of its aggregation. Baicalein is an electro-active flavonoid that can act as a metal-chelator and form several products including quinones upon oxidation. Exposure to Cu(II) ions is known to cause significant acceleration in the rate of α-synuclein fibril formation. Square-wave voltammetry (SWV) of α-synuclein in the presence of these electro-active factors revealed distinct interfacial changes attributed to complex formation of α-synuclein with these species in vitro. The role of baicalein as a fibrillogenesis inhibitor was found to be most effective during the early stages of the fibril formation. The proof-of-principal results indicate that electrochemistry as a drug screening technique can provide a powerful tool for the discovery of new fibrillogenesis inhibitors as promising therapeutics for neurodegenerative diseases.</s0>
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<s5>02</s5>
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<s2>NC</s2>
<s5>02</s5>
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<s2>NC</s2>
<s5>02</s5>
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<s5>03</s5>
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<s5>03</s5>
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<s5>04</s5>
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<s5>05</s5>
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<s5>05</s5>
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<s5>06</s5>
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<s5>06</s5>
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<s5>07</s5>
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<s5>07</s5>
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<s5>07</s5>
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<s5>08</s5>
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<s5>08</s5>
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<s5>08</s5>
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<s5>10</s5>
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<s5>10</s5>
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<fC03 i1="11" i2="X" l="FRE"><s0>Dérivé de la flavone</s0>
<s2>NK</s2>
<s5>32</s5>
</fC03>
<fC03 i1="11" i2="X" l="ENG"><s0>Flavone derivatives</s0>
<s2>NK</s2>
<s5>32</s5>
</fC03>
<fC03 i1="11" i2="X" l="SPA"><s0>Flavona derivado</s0>
<s2>NK</s2>
<s5>32</s5>
</fC03>
<fC03 i1="12" i2="X" l="FRE"><s0>Protéine</s0>
<s5>33</s5>
</fC03>
<fC03 i1="12" i2="X" l="ENG"><s0>Protein</s0>
<s5>33</s5>
</fC03>
<fC03 i1="12" i2="X" l="SPA"><s0>Proteína</s0>
<s5>33</s5>
</fC03>
<fC07 i1="01" i2="X" l="FRE"><s0>Flavonoïde</s0>
</fC07>
<fC07 i1="01" i2="X" l="ENG"><s0>Flavonoid</s0>
</fC07>
<fC07 i1="01" i2="X" l="SPA"><s0>Flavonoide</s0>
</fC07>
<fC07 i1="02" i2="X" l="FRE"><s0>Métal transition</s0>
<s2>NC</s2>
<s5>53</s5>
</fC07>
<fC07 i1="02" i2="X" l="ENG"><s0>Transition metal</s0>
<s2>NC</s2>
<s5>53</s5>
</fC07>
<fC07 i1="02" i2="X" l="SPA"><s0>Metal transición</s0>
<s2>NC</s2>
<s5>53</s5>
</fC07>
<fN21><s1>101</s1>
</fN21>
</pA>
</standard>
</inist>
<affiliations><list><country><li>Canada</li>
</country>
</list>
<tree><country name="Canada"><noRegion><name sortKey="Chan, Tiffiny" sort="Chan, Tiffiny" uniqKey="Chan T" first="Tiffiny" last="Chan">Tiffiny Chan</name>
</noRegion>
<name sortKey="Brown, Ian R" sort="Brown, Ian R" uniqKey="Brown I" first="Ian R." last="Brown">Ian R. Brown</name>
<name sortKey="Chow, Arim" sort="Chow, Arim" uniqKey="Chow A" first="Arim." last="Chow">Arim. Chow</name>
<name sortKey="Kerman, Kagan" sort="Kerman, Kagan" uniqKey="Kerman K" first="Kagan" last="Kerman">Kagan Kerman</name>
<name sortKey="Qi Li" sort="Qi Li" uniqKey="Qi Li" last="Qi Li">QI LI</name>
<name sortKey="Tang, Derekw F" sort="Tang, Derekw F" uniqKey="Tang D" first="Derekw. F." last="Tang">Derekw. F. Tang</name>
<name sortKey="Xuanyuanwang" sort="Xuanyuanwang" uniqKey="Xuanyuanwang" last="Xuanyuanwang">XUANYUANWANG</name>
</country>
</tree>
</affiliations>
</record>

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{{Explor lien
   |wiki=    Wicri/Canada
   |area=    ParkinsonCanadaV1
   |flux=    PascalFrancis
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   |type=    RBID
   |clé=     Pascal:11-0156674
   |texte=   Interaction of baicalein and copper with α-synuclein: Electrochemical approach to Parkinson's Disease
}}

This area was generated with Dilib version V0.6.29.
Data generation: Thu May 4 22:20:19 2017. Site generation: Fri Dec 23 23:17:26 2022

	La maladie de Parkinson au Canada (serveur d'exploration)
	Attention, ce site est en cours de développement ! Attention, site généré par des moyens informatiques à partir de corpus bruts. Les informations ne sont donc pas validées.

La maladie de Parkinson au Canada (serveur d'exploration)

Interaction of baicalein and copper with α-synuclein: Electrochemical approach to Parkinson's Disease

Interaction of baicalein and copper with α-synuclein: Electrochemical approach to Parkinson's Disease

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