Zinc-induced interaction of the metal-binding domain of amyloid-β peptide with DNA

J Alzheimers Dis. 2013;36(4):633-6. doi: 10.3233/JAD-130122.

Abstract

The interaction of the 16-mer synthetic peptide (Aβ16), which represents the metal-binding domain of the amyloid-β with DNA, was studied employing the surface plasmon resonance technique. It has been shown that Aβ16 binds to the duplex DNA in the presence of zinc ions and thus the metal-binding domain can serve as a zinc-dependent DNA-binding site of the amyloid-β. The interaction of Aβ16 with DNA most probably depends on oligomerization of the peptide and is dominated by interaction with phosphates of the DNA backbone.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amyloid beta-Peptides / metabolism*
  • Animals
  • Binding Sites / physiology
  • DNA / metabolism*
  • Humans
  • Peptide Fragments / metabolism*
  • Zinc / metabolism*

Substances

  • Amyloid beta-Peptides
  • Peptide Fragments
  • amyloid beta-protein (1-16)
  • DNA
  • Zinc