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Thermodynamics imprinting reveals differential binding of metals to a-synuclein: Relevance to parkinson’s disease

Ms., Bharathi and Rao, K.S.J. (2007) Thermodynamics imprinting reveals differential binding of metals to a-synuclein: Relevance to parkinson’s disease. Biochemical and Biophysical Research Communications, 359. pp. 115-120.

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Abstract

The aggregation of a-synuclein is a hallmark feature of Parkinson’s disease (PD) and other synucleinopathies. Metals are the significant etiological factors in PD, and their interaction with a-synuclein affect dramatically the kinetics of fibrillation in vitro and are proposed to play an important and potential neurodegenerative role in vivo. In the present study, we investigated the stoichiometry of binding of copper [Cu (II)] and iron [Fe (III)] with a-synuclein (wild recombinant type and A30P, A53T, E46K mutant forms) using isothermal titration calorimetry (ITC). a-Synuclein monomer (wild and mutant forms) titrated by Cu (II), showed two binding sites, with an apparent KB of 105 M and 104 M, respectively. But, a-synuclein (wild type and mutant forms) titrated with Fe (III) revealed a KB of 105 M with single binding site. The present investigation uncovers the detailed binding propensities between metals and a-synuclein and has biological implications in PD.

Item Type: Article
Uncontrolled Keywords: a-Synuclein; Copper; Iron; Wild type; Mutant forms; Thermodynamics; Isothermal titration calorimetry; Binding sites
Subjects: 600 Technology > 01 Medical sciences
Divisions: Dept. of Biochemistry
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 20 Nov 2008 07:15
Last Modified: 11 May 2012 03:48
URI: http://ir.cftri.com/id/eprint/8851

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