Zinc-Induced Interaction of the Metal-Binding Domain of Amyloid-β Peptide with DNA

Article type: Short Communication

Authors: Khmeleva, Svetlana A.^a | Mezentsev, Yuri V.^a | Kozin, Sergey A.^{a; b} | Tsvetkov, Philipp O.^b | Ivanov, Alexis S.^a | Bodoev, Nikolay V.^a | Makarov, Alexander A.^b | Radko, Sergey P.^{a; b; *}

Affiliations: [a] Orekhovich Institute of Biomedical Chemistry, Russian Academy of Medical Sciences, Moscow, Russia | [b] Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia

Correspondence: [*] Correspondence to: Sergey P. Radko and Sergey A. Kozin, Orekhovich Institute of Biomedical Chemistry, Russian Academy of Medical Sciences, Moscow, Russia. Tel.: +7 499 2457115; Fax: +7 499 2450857; E-mails: radko@ibmc.msk.ru (S.P. Radko); kozinsa@gmail.com (S.A. Kozin).

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.

Keywords: Alzheimer's disease, amyloid-β peptide, DNA, zinc

DOI: 10.3233/JAD-130122

Journal: Journal of Alzheimer's Disease, vol. 36, no. 4, pp. 633-636, 2013