Cu(II) Affinity for the Alzheimer's Peptide: Tyrosine Fluorescence Studies Revisited

被引：144

作者：

Alies, Bruno ^{[1
,2
]}

Renaglia, Emelyne ^{[1
,2
]}

Rozga, Malgorzata ^{[3
]}

Bal, Wojciech ^{[3
]}

Faller, Peter ^{[1
,2
]}

Hureau, Christelle ^{[1
,2
]}

机构：

[1] CNRS, LCC, F-31077 Toulouse 4, France

[2] Univ Toulouse, UPS, INPT, LCC, F-31077 Toulouse, France

[3] Polish Acad Sci, Inst Biochem & Biophys, PL-02106 Warsaw, Poland

来源：

ANALYTICAL CHEMISTRY | 2013年 / 85卷 / 03期

关键词：

AMYLOID-BETA-PEPTIDE; ACTIVE METAL-IONS; A-BETA; ALPHA-SYNUCLEIN; BINDING-SITE; NEURODEGENERATIVE DISORDERS; BIOINORGANIC CHEMISTRY; COORDINATION GEOMETRY; PRECURSOR PROTEIN; COPPER-BINDING;

D O I：

10.1021/ac302629u

中图分类号：

O65 [分析化学];

学科分类号：

070302 ; 081704 ;

摘要：

Copper(II) binding to the amyloid-beta peptide has been proposed to be a key event in the cascade leading to Alzheimer's disease. As a direct consequence, the strength of the Cu(II) to A beta interaction, that is, the Cu(II) affinity of A beta, is a very important parameter to determine. Because A beta peptide contain one Tyr fluorophore in its sequence and because Cu(II) does quench Tyr fluorescence, fluorescence measurements appear to be a straightforward way to obtain this parameter. However, this proved to be wrong, mainly because of data misinterpretation in some previous studies that leads to a conflicting situation. In the present paper, we have investigated in details a large set of fluorescence data that were analyzed with a new method taking into account the presence of two Cu(II) sites and the inner-filter effect. This leads to reinterpretation of the published data and to the determination of a unified affinity value in the 10(10) M-1 range.

引用

页码：1501 / 1508

页数：8

共 49 条

[21] Coordination of redox active metal ions to the amyloid precursor protein and to amyloid-β peptides involved in Alzheimer disease. Part 2: Dependence of Cu(II) binding sites with Aβ sequences [J].