Histidine availability is decisive in ROS-mediated cytotoxicity of copper complexes of Aβ1-16 peptide

Yamini P. Ginotra, Shefali N. Ramteke, Gulshan R. Walke, Srikanth Rapole, Prasad P. Kulkarni

Research output: Contribution to journalArticlepeer-review

11 Scopus citations


The binding of metal ions to Aβ peptide plays an important role in the etiology of AD. Copper coordinates chiefly to His residues and produces reactive oxygen species (ROS) upon redox cycling. ROS builds enormous burden on the normal functioning of neuronal cells and results into deleterious effects. Recently, two structurally distinct copper binding sites with contrasting redox properties were characterized. Here, we demonstrate for the first time the effect of binding of two equivalents of Cu2+ on redox properties and cytotoxicity of Aβ peptide. Our electrochemical data and ascorbate consumption assay suggest that in the presence of two equivalents of copper; Aβ peptide has higher propensity of H2O2 generation. The oxidation of Aβ1-16 peptide due to both gamma radiolysis and metal catalyzed oxidation in the presence of two equivalents of copper is inhibited confirming the binding of both equivalents of copper to peptide. The electrochemical and cytotoxicity study shows that negative shift in the reduction potential is reflected as slightly higher cytotoxicity in SH-SY5Y cell lines for Aβ1-16-Cu2+ (1:2) complex.

Original languageEnglish
Pages (from-to)405-413
Number of pages9
JournalFree Radical Research
Issue number4
StatePublished - 2 Apr 2016
Externally publishedYes

Bibliographical note

Publisher Copyright:
© 2016 Taylor and Francis.


  • Alzheimers disease
  • amyloid β
  • copper
  • cytotoxicity
  • reactive oxygen species


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