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

被引：11

作者：

Khmeleva, Svetlana A. ^{[1
]}

Mezentsev, Yuri V. ^{[1
]}

Kozin, Sergey A. ^{[1
,2
]}

Tsvetkov, Philipp O. ^{[2
]}

Ivanov, Alexis S. ^{[1
]}

Bodoev, Nikolay V. ^{[1
]}

Makarov, Alexander A. ^{[2
]}

Radko, Sergey P. ^{[1
,2
]}

机构：

[1] Russian Acad Med Sci, Orekhovich Inst Biomed Chem, Moscow, Russia

[2] Russian Acad Sci, VA Engelhardt Mol Biol Inst, Moscow, Russia

来源：

JOURNAL OF ALZHEIMERS DISEASE | 2013年 / 36卷 / 04期

基金：

俄罗斯基础研究基金会;

关键词：

Alzheimer's disease; amyloid-beta peptide; DNA; zinc; A-BETA; AGGREGATION; COPPER; PROMOTER; ZN2+; SITE;

D O I：

10.3233/JAD-130122

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

The interaction of the 16-mer synthetic peptide (A beta(16)), which represents the metal-binding domain of the amyloid-beta with DNA, was studied employing the surface plasmon resonance technique. It has been shown that A beta(16) 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-beta. The interaction of A beta(16) with DNA most probably depends on oligomerization of the peptide and is dominated by interaction with phosphates of the DNA backbone.

引用

页码：633 / 636

页数：4

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