Cu(II)-Zn(II) Cross-Modulation in Amyloid-Beta Peptide Binding: An X-ray Absorption Spectroscopy Study.
Cu(II)-Zn(II) Cross-Modulation in Amyloid-Beta Peptide Binding: An X-ray Absorption Spectroscopy Study.
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DOI：
10.1021/acs.jpcb.5b10264
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发表时间：
2015-12-31
期刊：
影响因子：
--
通讯作者：
Morante S
中科院分区：
文献类型：
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作者：
De Santis E;Minicozzi V;Proux O;Rossi G;Silva KI;Lawless MJ;Stellato F;Saxena S;Morante S
在这项工作中，我们在结构水平上分析了 Cu(II) 和 Zn(II) 离子竞争与 Aβ 肽结合的机制，而 Aβ 肽与阿尔茨海默病的病因有关。我们收集了含有不同浓度比例的 Aβ 与 Cu 和 Zn 的样品的 X 射线吸收光谱数据。我们证明金属添加到肽溶液中的顺序很重要，并且当首先添加 Zn 时，它会阻止 Cu 结合。相反，当首先添加 Cu 时，它不会（完全）阻止 Zn 与 Aβ 肽的结合。我们的分析表明，Cu 和 Zn 离子根据 [离子]:[肽] 浓度比与不同数量的组氨酸残基配位。
In this work we analyze at a structural level the mechanism by which Cu(II) and Zn(II) ions compete for binding to the Aβ peptides that is involved in the etiology of Alzheimer’s disease. We collected X-ray Absorption Spectroscopy data on samples containing Aβ with Cu and Zn at different concentration ratios. We show that the order in which metals are added to the peptide solution matters and that, when Zn is added first, it prevents Cu from binding. On the contrary, when Cu is added first, it does not (completely) prevent Zn binding to Aβ peptides. Our analysis suggests that Cu and Zn ions are coordinated to different numbers of histidine residues depending on the [ion]:[peptide] concentration ratio.