淀粉样β肽结合中的铜（II）-锌（II）交叉调制：一项X射线吸收光谱研究。
Cu(II)-Zn(II) Cross-Modulation in Amyloid-Beta Peptide Binding: An X-ray Absorption Spectroscopy Study.
作者信息
De Santis Emiliano, Minicozzi Velia, Proux Olivier, Rossi Giancarlo, Silva K Ishara, Lawless Matthew J, Stellato Francesco, Saxena Sunil, Morante Silvia
机构信息
Department of Physics and INFN, University of Rome , Tor Vergata, Rome 00133, Italy.
Observatoire des Sciences de l'Univers de Grenoble , Grenoble 38400, France.
出版信息
J Phys Chem B. 2015 Dec 31;119(52):15813-20. doi: 10.1021/acs.jpcb.5b10264. Epub 2015 Dec 21.
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.
在这项工作中，我们从结构层面分析了铜（II）离子和锌（II）离子竞争与参与阿尔茨海默病病因的Aβ肽结合的机制。我们收集了不同浓度比的含铜和锌的Aβ样品的X射线吸收光谱数据。我们发现，向肽溶液中添加金属的顺序很重要，并且当首先添加锌时，它会阻止铜结合。相反，当首先添加铜时，它不会（完全）阻止锌与Aβ肽结合。我们的分析表明，根据[离子]：[肽]浓度比，铜离子和锌离子与不同数量的组氨酸残基配位。
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