Structural and thermodynamical properties of CuII amyloid-β16/28 complexes associated with Alzheimer's disease

被引:121
作者
Guilloreau, Luc
Damian, Luminita
Coppel, Yannick
Mazarguil, Honore
Winterhalter, Mathias
Faller, Peter
机构
[1] Univ Toulouse 3, Chim Coordinat Lab, CNRS UPR 8241, F-31077 Toulouse 4, France
[2] Inst Pharmacol & Biol Struct, F-31077 Toulouse, France
[3] Int Univ Bremen, D-20725 Bremen, Germany
来源
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY | 2006年 / 11卷 / 08期
关键词
copper; beta-amyloid; calorimetry; spectroscopy; coordination;
D O I
10.1007/s00775-006-0154-1
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The aggregation of the peptide amyloid-beta (A beta) to form amyloid plaques is a key event in Alzheimer's disease. It has been shown that Cull can bind to soluble A beta and influence its aggregation properties. Three histidines and the N-terminal amine have been proposed to be involved in its coordination. Here, for the first time, we show isothermal titration calorimetry (ITC) measurements of the Cull binding to A beta 16 and A beta 28, models of the soluble A beta. Moreover, different spectroscopic methods were applied. The studies revealed new insights into these Cu-II-A beta complexes: (1) ITC showed two Cull binding sites, with an apparent K-d of 10(-7) and 10(-5) M, respectively; (2) the high-affinity site has a smaller enthalpic contribution but a larger entropic contribution than the low-affinity binding site; (3) azide did not bind to Cull in the higher-affinity binding site, suggesting the absence of a weak, labile ligand; (4) azide could bind to the Cull in the low-affinity binding site in A beta 28 but not in A beta 16; (5) H-1-NMR suggests that the carboxylate of aspartic acid in position 1 is involved in the ligation to Cull in the high-affinity binding site; (6) the pK(a) of 11.3 of tyrosine in position 10 was not influenced by the binding of 2 equivalents of Cu-II.
引用
收藏
页码:1024 / 1038
页数:15
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