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

Ms., Bharathi and Rao, K.S.J. (2008) Molecular Understanding of Copper and Iron Interaction with alpha-Synuclein by Fluorescence Analysis. Journal of Molecular Neuroscience, 35. pp. 273-281. ISSN 0895-8696

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Abstract

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.

Item Type: Article
Uncontrolled Keywords: α-Synuclein . Copper . Iron . Intrinsic tyrosine fluorescence . Binding . Fibrillogenesis
Subjects: 600 Technology > 01 Medical sciences
Divisions: Dept. of Biochemistry
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 07 Jun 2011 06:58
Last Modified: 28 Dec 2011 09:34
URI: http://ir.cftri.com/id/eprint/1784

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