Electroanalysis of the interaction between (-)-epigallocatechin-3-gallate (EGCG) and amyloid-β in the presence of copper.

Biao Zhang, Xin R Cheng, Iranaldo S da Silva, Vinci W S Hung, Anthony J Veloso, Lúcio Angnes, Kagan Kerman

Department of Physical and Environmental Sciences, University of Toronto Scarborough, Toronto, ON, Canada.

Metallomics : integrated biometal science 2013 Mar

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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.

Citation

Biao Zhang, Xin R Cheng, Iranaldo S da Silva, Vinci W S Hung, Anthony J Veloso, Lúcio Angnes, Kagan Kerman. Electroanalysis of the interaction between (-)-epigallocatechin-3-gallate (EGCG) and amyloid-β in the presence of copper. Metallomics : integrated biometal science. 2013 Mar;5(3):259-64