首页> 外文期刊>The journal of physical chemistry, B. Condensed matter, materials, surfaces, interfaces & biophysical >Cu(II)-Zn(II) Cross-Modulation in Amyloid-Beta Peptide Binding: An X-ray Absorption Spectroscopy Study
【24h】

Cu(II)-Zn(II) Cross-Modulation in Amyloid-Beta Peptide Binding: An X-ray Absorption Spectroscopy Study

机译:淀粉样β肽结合中的铜(II)-锌(II)交叉调制:X射线吸收光谱研究。

获取原文
获取原文并翻译 | 示例
           

摘要

In this work we analyze at a structural level the mechanism by which Cu(II) and Zn(II) ions compete for binding to the A beta peptides that is involved in the etiology of Alzheimer's disease. We collected X-ray absorption spectroscopy data on samples containing A beta 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 A beta peptides. Our analysis suggests that Cu and Zn ions are coordinated to different numbers of histidine residues depending on the [ion]:[peptide] concentration ratio.
机译: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Alzheimer病病因相关的Aβ肽结合的机制。我们收集了含有不同浓度比率的A beta与Cu和Zn的样品的X射线吸收光谱数据。我们表明,将金属添加到肽溶液中的顺序很重要,并且当首先添加Zn时,它可以防止Cu结合。相反,当首先添加Cu时,它不能(完全)阻止Zn与A beta肽的结合。我们的分析表明,铜和锌离子根据[离子]:[肽]的浓度比与不同数量的组氨酸残基配位。

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号