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Cu K 边缘 X 射线吸收光谱显示，与单体相比，淀粉样β寡聚体中的铜配位存在差异。

Cu K-edge X-ray absorption spectroscopy reveals differential copper coordination within amyloid-β oligomers compared to amyloid-β monomers.

机构信息

Department of Chemistry, University of Nevada, Reno, NV 89557, USA.

出版信息

Chem Commun (Camb). 2010 Dec 28;46(48):9137-9. doi: 10.1039/c0cc02446e. Epub 2010 Nov 8.

DOI:10.1039/c0cc02446e
PMID:21060917
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3082590/
Abstract

The fatal neurological disorder Alzheimer's disease has been linked to soluble neurotoxic oligomers of amyloid-β (Aβ) peptides. Herein we demonstrate that Cu(1+) ligated within Aβ(42) oligomers (Aβ sequence: DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA) possesses a highly dioxygen sensitive tetrahedral coordination geometry. The biological implications of these findings are discussed.

摘要

致命的神经紊乱疾病阿尔茨海默病与淀粉样β（Aβ）肽的可溶性神经毒性低聚物有关。在此，我们证明了在 Aβ（42）低聚物（Aβ 序列：DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA）中配位的 Cu（1+）具有高度敏感的双氧四面配位几何构型。讨论了这些发现的生物学意义。

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本文引用的文献

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Affinity of Cu+ for the copper-binding domain of the amyloid-β peptide of Alzheimer's disease.阿尔茨海默病淀粉样β肽的铜结合域与 Cu+的亲和力。
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The amyloid-beta peptide of Alzheimer's disease binds Cu(I) in a linear bis-his coordination environment: insight into a possible neuroprotective mechanism for the amyloid-beta peptide.阿尔茨海默病的β-淀粉样肽在一个线性双组氨酸配位环境中结合Cu(I)：对β-淀粉样肽可能的神经保护机制的深入了解。
J Am Chem Soc. 2008 Dec 31;130(52):17826-35. doi: 10.1021/ja805940m.
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Global prevalence of dementia: a Delphi consensus study.痴呆症的全球患病率：一项德尔菲共识研究。
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