Effects of oxidation on redox and cytotoxic properties of copper complex of Aβ1-16 peptide

S. N. Ramteke, G. R. Walke, B. N. Joshi, S. Rapole, P. P. Kulkarni

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

The effect of oxidation on redox and cytotoxic properties of copper complex of amyloid beta (Aβ) peptide was studied by gamma radiolysis. The oxidation of Aβ1-16 and Aβ1-16/Cu(II) complex was carried out using hydroxyl (OH) radicals produced by gamma radiolysis and the products were analyzed using mass spectrometry. The presence of Cu(II) was found to enhance the oxidation of Aβ1-16 peptide. The oxidation of residues Asp1, His6, and His13 was enhanced due to their involvement in copper binding. The oxidation of His residues of Aβ1-16 peptide, which are chiefly responsible for copper binding, resulted in altered redox properties and subsequently in higher cytotoxicity of the Aβ1-16 peptide in SH-SY5Y cells.

Original languageEnglish
Pages (from-to)1417-1425
Number of pages9
JournalFree Radical Research
Volume48
Issue number12
DOIs
StatePublished - 1 Dec 2014
Externally publishedYes

Bibliographical note

Publisher Copyright:
© 2014 Informa UK, Ltd.

Keywords

  • Amyloid β
  • Copper
  • Free radicals
  • Gamma radiolysis
  • Mass spectrometry

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