CNRS, LCC (Laboratoire de Chimie de Coordination), 205, route de Narbonne, F-31077 Toulouse, France.
Inorg Chem. 2011 Nov 7;50(21):11192-201. doi: 10.1021/ic201739n. Epub 2011 Oct 6.
Copper ions have been proposed to intervene in deleterious processes linked to the development of Alzheimer's disease (AD). As a direct consequence, delineating how Cu(II) can be bound to amyloid-β (Aβ) peptide, the amyloidogenic peptide encountered in AD, is of paramount importance. Two different forms of [Cu(II)(Aβ)] complexes are present near physiological pH, usually noted components I and II, the nature of which is still widely debated in the literature, especially for II. In the present report, the phenomenological pH-dependent study of Cu(II) coordination to Aβ and to ten mutants by EPR, CD, and NMR techniques is described. Although only indirect insights can be obtained from the study of Cu(II) binding to mutated peptides, they reveal very useful for better defining Cu(II) coordination sites in the native Aβ peptide. Four components were identified between pH 6 and 12, namely, components I, II, III and IV, in which the predominant Cu(II) equatorial sites are {-NH(2), CO (Asp1-Ala2), N(im) (His6), N(im) (His13 or His14)}, {-NH(2), N(-) (Asp1-Ala2), CO (Ala2-Glu3), N(im)}, {-NH(2), N(-) (Asp1-Ala2), N(-) (Ala2-Glu3), N(im)} and {-NH(2), N(-) (Asp1-Ala2), N(-) (Ala2-Glu3), N(-) (Glu3-Phe4)}, respectively, in line with classical pH-induced deprotonation of the peptide backbone encountered in Cu(II) peptidic complexes formation. The structure proposed for component II is discussed with respect to another coordination model reported in the literature, that is, {CO (Ala2-Glu3), 3 N(im)}. Cu(II) binding to the H6R-Aβ and D7N-Aβ peptides, where the familial H6R and D7N mutations have been linked to early onset of AD, has also been investigated. In case of the H6R mutation, some different structural features (compared to those encountered in the native [Cu(II)(Aβ)] species) have been evidenced and are anticipated to be important for the aggregating properties of the H6R-Aβ peptide in presence of Cu(II).
铜离子被认为可以干预阿尔茨海默病(AD)发展过程中的有害过程。因此,描述 Cu(II)如何与淀粉样β肽(Aβ)结合,这种肽在 AD 中遇到,是至关重要的。在生理 pH 附近存在两种不同形式的 [Cu(II)(Aβ)] 配合物,通常标记为 I 型和 II 型,其性质在文献中仍存在广泛争议,尤其是对于 II 型。在本报告中,通过 EPR、CD 和 NMR 技术描述了铜(II)与 Aβ及其十个突变体在 pH 依赖性方面的配位情况。尽管从突变肽的铜(II)结合研究中只能获得间接的见解,但它们对于更好地定义天然 Aβ肽中的 Cu(II)配位位点非常有用。在 pH 6 到 12 之间鉴定出了四种组分,即 I、II、III 和 IV 型,其中 Cu(II)的主要配位体为 {-NH(2),CO(Asp1-Ala2),N(im)(His6),N(im)(His13 或 His14)}、{-NH(2),N(-)(Asp1-Ala2),CO(Ala2-Glu3),N(im)}、{-NH(2),N(-)(Asp1-Ala2),N(-)(Ala2-Glu3),N(im)} 和 {-NH(2),N(-)(Asp1-Ala2),N(-)(Ala2-Glu3),N(-)(Glu3-Phe4)},与在 Cu(II)肽配合物形成中遇到的经典 pH 诱导的肽骨架去质子化一致。讨论了与文献中报道的另一种配位模型(即 CO(Ala2-Glu3),3 N(im))相对应的 II 型结构。还研究了与早发性 AD 相关的家族性 H6R 和 D7N 突变的 H6R-Aβ 和 D7N-Aβ 肽的 Cu(II)结合情况。对于 H6R 突变,已经证明了一些不同的结构特征(与天然 [Cu(II)(Aβ)] 物种相比),预计这些特征对于 H6R-Aβ 肽在 Cu(II)存在下的聚集性质很重要。