title: Electroanalysis of the interaction between (-)-epigallocatechin-3-gallate (EGCG) and amyloid-β in the presence of copper.
abstract: The misfolding of amyloid-beta (Aβ) peptide is one of the pathological hallmarks of Alzheimer's disease (AD). Polyphenols are strong antioxidants and metal chelators, with characteristics that are of beneficial therapeutic values for their development as candidates targeting neurodegenerative and metal-induced diseases. We have demonstrated here the electrochemical properties of a green tea component, (-)-epigallocatechin-3-gallate (EGCG), and its potent activity on Aβ peptides. Characterization of early interactions (≤48 h) between EGCG and Aβ was conducted using square wave voltammetry (SWV). The interaction of Cu(ii) ions with the Tyr-10 residue of Aβ was shown to be affected by surrounding His residues. Morphological changes due to the binding of EGCG and Cu(II) were also elucidated using transmission electron microscopy (TEM). Electroanalytical techniques are promising for facilitating the investigation of metals and flavonoids in drug screening studies.
authors: Department of Physical and Environmental Sciences, University of Toronto Scarborough, Toronto, ON, Canada.
authors: Biao
authors: B
authors: Zhang
authors: Xin R
authors: XR
authors: Cheng
authors: Iranaldo S
authors: IS
authors: da Silva
authors: Vinci W S
authors: VW
authors: Hung
authors: Anthony J
authors: AJ
authors: Veloso
authors: Lúcio
authors: L
authors: Angnes
authors: Kagan
authors: K
authors: Kerman
mesh_terms: D016229:Amyloid beta-Peptides / Q000737:chemistry*; D002392:Catechin / Q000031:analogs & derivatives* / Q000737:chemistry; D003300:Copper / Q000737:chemistry* / Q000494:pharmacology; D046529:Microscopy, Electron, Transmission; D011485:Protein Binding / Q000187:drug effects
chemical_list: D016229:Amyloid beta-Peptides; D003300:Copper; D002392:Catechin; C045651:epigallocatechin gallate