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

Chan, Tiffiny; Chow, Ari M.; Tang, Derek W. F.; Li, Qi; Wang, Xuanyuan; Brown, Ian R.; Kerman, Kağan

doi:10.1016/j.jelechem.2010.07.015

Cited by 26 publications

(29 citation statements)

References 42 publications

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“…5, electrochemical assessment of Ab1-42 aggregation kinetics supported this hypothesis, as the decrease was most significant for the incubation with Ab1-42 alone, and plateaued shortly after 200 min passed. A similar phenomenon has been reported recently, 42 when baicalein was incubated with a-synuclein, another amyloidogenic protein, and thus, confirmed the validity of our electrochemical analysis.…”

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confidence: 91%

Label-free methods for probing the interaction of clioquinol with amyloid-β

et al. 2012

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The presence of amyloid-b (Ab) fibrils is characteristic of Alzheimer's disease (AD), and the aggregation of these amyloidogenic proteins is a nucleation-dependent process. In this report, label-free methods based on surface plasmon resonance (SPR) and thickness shear mode acoustic wave sensors (TSM-AWS) were used to detect monomer elongation in real-time. The modulation of Ab aggregation using a well-described flavonoid, clioquinol (CQ) was also observed. Established methods like fluorescence and electrochemistry were also employed to confirm the interaction of CQ with Ab. Good correlation between the designed label-free methods creates a promising platform for the screening of novel amyloid inhibitors.

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confidence: 91%

Label-free methods for probing the interaction of clioquinol with amyloid-β

et al. 2012

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“…However, the aggregation kinetics was quite different. For example, the addition of Cu to a-synuclein caused a dramatic decrease in Tyr oxidation signal and the aggregation pathway followed a similar course to the aggregation occurring in the absence of Cu after 10 h [79].…”

Section: Comparison Of Fe Cu and Zn's Influence On Ab Aggregationmentioning

confidence: 86%

“…Overall, all the metal ions analyzed in this study were able to modulate the aggregation kinetics of Ab in vitro, but the general stability of the aggregates formed still seemed to be reliant on the presence of the hydrophobic region found in Ab42, but not in Ab16. Similarly, research has also been done on another type of amyloidogenic protein, a-synuclein and it was found that Cu and Fe were able to accelerate its aggregation and eventual formation of fibrils [79,80]. However, the aggregation kinetics was quite different.…”

Section: Comparison Of Fe Cu and Zn's Influence On Ab Aggregationmentioning

confidence: 99%

Label-free electrochemical detection of Amyloid beta aggregation in the presence of iron, copper and zinc

Hung

Masoom

Kerman

2012

Journal of Electroanalytical Chemistry

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“…Although the biological role of Cu(II) in neurodegenerative disorders has been extensively examined, studies on the biological role of Cu(I) are relatively scarce . Cu(I) plays a central role in Wilson's disease, which is characterized by the toxic accumulation of copper in the liver and then in extrahepatic sites .…”

Section: Copper and Neurodegenerative Disordersmentioning

confidence: 99%

Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases

Emwas

Al‐Talla

Guo

et al. 2013

Magnetic Reson in Chemistry

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Copper is an essential nutrient for the normal development of the brain and nervous system, although the hallmark of several neurological diseases is a change in copper concentrations in the brain and central nervous system. Prion protein (PrP) is a copper-binding, cell-surface glycoprotein that exists in two alternatively folded conformations: a normal isoform (PrP(C)) and a disease-associated isoform (PrP(Sc)). Prion diseases are a group of lethal neurodegenerative disorders that develop as a result of conformational conversion of PrP(C) into PrP(Sc). The pathogenic mechanism that triggers this conformational transformation with the subsequent development of prion diseases remains unclear. It has, however, been shown repeatedly that copper plays a significant functional role in the conformational conversion of prion proteins. In this review, we focus on current research that seeks to clarify the conformational changes associated with prion diseases and the role of copper in this mechanism, with emphasis on the latest applications of NMR and EPR spectroscopy to probe the interactions of copper with prion proteins.

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

Cited by 26 publications

References 42 publications

Label-free methods for probing the interaction of clioquinol with amyloid-β

Label-free methods for probing the interaction of clioquinol with amyloid-β

Label-free electrochemical detection of Amyloid beta aggregation in the presence of iron, copper and zinc

Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases

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