, Volume 35, Issue 3, pp 273-281
Date: 20 May 2008

Molecular Understanding of Copper and Iron Interaction with α-Synuclein by Fluorescence Analysis

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α-Synuclein aggregation is a hallmark pathological feature in Parkinson’s disease (PD). The conversion of α-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 α-synuclein fibrillogenesis. In the present investigation, we analyzed the binding efficiency of Cu and Fe to α-synuclein by fluorescence studies. It is interesting to note that Cu and Fe showed differential binding pattern toward α-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 α-synuclein and its role in neurodegeneration.