Copper(II), nickel(II) and zinc(II) complexes of the N-terminal nonapeptide fragment of amyloid-β and its derivatives

Ágnes Grenács, Imre Sóvágó

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

Copper(II), nickel(II) and zinc(II) complexes of the nonapeptide fragment of amyloid-β Aβ(1-9) (NH2-DAEFRHDSG-NH2) and its two derivatives: NH2-DAAAAHAAA-NH2 and NH 2-DAAAAAHAA-NH2 have been studied by potentiometric, UV-visible and CD spectroscopic methods. The results reveal the primary role of the amino terminus of peptides in copper(II) and nickel(II) binding. The formation of dinuclear complexes was also possible in the copper(II) containing systems but only the first six amino acids from the amino terminus were involved in metal binding in the physiologically relevant pH range. The coordination chemistry of the two alanine mutated peptides is almost the same as that of the native nonapeptide, but the thermodynamic stability of the copper(II) complexes of the mutants is significantly reduced. This difference probably comes from the secondary interactions of the polar side chains of Asp, Glu, Ser and Arg residues present in the native peptide. Moreover, this difference reveals that the amino acid sequence of the N-terminal domains of amyloid peptides is especially well suited for the complexation with copper(II) ions.

Original languageEnglish
Pages (from-to)49-56
Number of pages8
JournalJournal of Inorganic Biochemistry
Volume139
DOIs
Publication statusPublished - Oct 2014

Keywords

  • Amyloid-β
  • CD spectroscopy
  • Copper(II)
  • Nickel(II)
  • Stability constants
  • Zinc(II)

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry

Fingerprint Dive into the research topics of 'Copper(II), nickel(II) and zinc(II) complexes of the N-terminal nonapeptide fragment of amyloid-β and its derivatives'. Together they form a unique fingerprint.

  • Cite this