Binding of iron(III) to the single tyrosine residue of amyloid β-peptide probed by raman spectroscopy

Takashi Miura, Kiyoko Suzuki, Hideo Takeuchi

Research output: Contribution to journalArticlepeer-review

41 Citations (Scopus)

Abstract

The Fe(III) ion binds to amyloid β-peptide (Aβ) and induces significant aggregation of the peptide. In addition to the Aβ aggregation, the redox activity of the Fe(III) ion bound to Aβ is considered to play a role in the pathogenesis of Alzheimer's disease. In order to understand the role of Fe(III) in Aβ aggregation and neurotoxicity, we have examined the Fe(III)-binding mode of human Aβ by Raman spectroscopy. The Raman spectra of Fe(III)-Aβ complexes excited at 514.5 nm are dominated by resonance Raman bands of metal-bound tyrosinate, evidencing that the Fe(III) ion primarily binds to Aβ via the phenolic oxygen of Tyr10. In addition, carboxylate groups of glutamate/aspartate side chains are also bound to Fe(III). On the other hand, histidine residues in the N-terminal hydrophilic region of Aβ do not bind to Fe(III). These results are in sharp contrast to the Zn(II)- or Cu(II)-induced aggregation of Aβ, in which histidine residues act as the primary metal binding sites. The Fe(III)-- Tyr10 binding may play an important role in Aβ aggregation and in decreasing the reduction potential of the bound Fe(III) ion.

Original languageEnglish
Pages (from-to)79-84
Number of pages6
JournalJournal of Molecular Structure
Volume598
Issue number1
DOIs
Publication statusPublished - 2001 Oct 31

Keywords

  • Amyloid β-peptide
  • Ferric ion
  • Metal ion
  • Raman spectroscopy
  • Tyrosinate

ASJC Scopus subject areas

  • Analytical Chemistry
  • Spectroscopy
  • Organic Chemistry
  • Inorganic Chemistry

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