College of Chemistry and Chemical Engineering, Anyang Normal University, Anyang, Henan, People's Republic of China.
Biochem Biophys Res Commun. 2012 Jan 6;417(1):153-6. doi: 10.1016/j.bbrc.2011.11.074. Epub 2011 Nov 23.
A growing body of Alzheimer's disease (AD) research is concerned with understanding the interaction between amyloid-β (Aβ) peptides and metal ions (e.g., Cu, Zn, and Fe) and determining the biological relevance of the metal-Aβ complexes to essential metal homeostasis and neuronal cell loss. Previously, many studies have dealt with the interaction between Aβ and "single" but not "multiple" metal ions in terms of binding affinity and coordination chemistry. In the present work, we found that Zn(II) ions modified the configuration of Aβ-Cu(II) by forming Zn(II)-Aβ-Cu(II) ternary complexes. As a result, the catalytic activity of Aβ-Cu(II) against a biological ascorbic acid species was repressed by Zn(II) binding. The formation of the ternary complex can therefore explain the protective role of Zn(II) in AD.
越来越多的阿尔茨海默病（AD）研究致力于理解淀粉样β（Aβ）肽与金属离子（例如 Cu、Zn 和 Fe）之间的相互作用，并确定金属-Aβ 配合物对必需金属动态平衡和神经元细胞丢失的生物学相关性。以前，许多研究都涉及 Aβ 与“单个”而非“多个”金属离子之间的相互作用，包括结合亲和力和配位化学。在本工作中，我们发现 Zn(II) 离子通过形成 Zn(II)-Aβ-Cu(II)三元配合物来修饰 Aβ-Cu(II)的构象。结果，Zn(II)结合抑制了 Aβ-Cu(II)对生物抗坏血酸物质的催化活性。因此，三元配合物的形成可以解释 Zn(II)在 AD 中的保护作用。
