Molecular understanding of copper and iron interaction with α-synuclein by fluorescence analysis

被引：13

作者：

Rao, Bharathi K. S. J. ^{[1
]}

机构：

[1] Cent Food Technol Res Inst, Dept Biochem & Nutr, Mysore 570020, Karnataka, India

来源：

JOURNAL OF MOLECULAR NEUROSCIENCE | 2008年 / 35卷 / 03期

关键词：

alpha-synuclein; copper; iron; intrinsic tyrosine fluorescence; binding; fibrillogenesis;

D O I：

10.1007/s12031-008-9076-4

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：

alpha-Synuclein aggregation is a hallmark pathological feature in Parkinson's disease (PD). The conversion of alpha-synuclein from a soluble monomer to an insoluble fibril may underlie the neurodegeneration associated with PD. Redox-active metal ions such as iron (Fe) and copper (Cu) are known to enhance alpha-synuclein fibrillogenesis. In the present investigation, we analyzed the binding efficiency of Cu and Fe to alpha-synuclein by fluorescence studies. It is interesting to note that Cu and Fe showed differential binding pattern toward alpha-synuclein (wild type and A30P, A53T, and E46K mutant forms) as revealed by intrinsic tyrosine fluorescence, thioflavin-T fluorescence, 1-anilino-8-naphthalenesulfonate-binding studies, and scatchard plot analysis. The experimental data might prove useful in understanding the hierarchy of metals binding to alpha-synuclein and its role in neurodegeneration.

引用

页码：273 / 281

页数：9

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