☆ 4.8 Article

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

ANALYTICAL CHEMISTRY (2013)

期刊

ANALYTICAL CHEMISTRY

卷 85, 期 3, 页码 1501-1508

出版社

AMER CHEMICAL SOC

DOI: 10.1021/ac302629u

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Chemistry, Analytical

资金

ANR (Agence Nationale de la Recherche) [NT09-488591]
National Centre for Science, Poland [2741/B/H03/2010/38]
Polish Ministry of Science and Higher Education [0463/IP1/2011/71]

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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.

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