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Copper- and iron-induced differential fibril formation in \alpha-synuclein: TEM study

Bharathi, * and Indi, SS and Rao, KSJ (2007) Copper- and iron-induced differential fibril formation in \alpha-synuclein: TEM study. In: Neuroscience Letters, 424 (2). pp. 78-82.

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\alpha-Synuclein filaments are the central component of intracytoplasmic inclusion bodies characteristic of Parkinson's disease (PD) and related disorders. Metals are the significant etiological factors in PD, and their interaction with \alpha-synuclein affect dramatically the kinetics of fibrillation. Currently, we have investigated the influence of Cu(II) and Fe(III) on \alpha-synuclein fibril formation. Cu(II) and Fe(III) selectively and differentially induced the formation of discrete \alpha-synuclein fibrillar species. Transmission electron microscopy was used to monitor the aggregation state of \alpha-synuclein (wild-type, A30P, A53T, and E46K) after 60 h with stirring at $37^{\circ}C$ in the presence and absence of metal ions. Cu(II) has induced thin long network-like fibrils with the wild-type of \alpha-synuclein, while the mutant, showed amorphous aggregates with no fibrillar forms. Fe(III) induced short and thick fibrils with both wild and mutant forms and were similar to \alpha-synuclein fibrils incubated without metal ion. The present study illustrates the metal-specific fibril morphology, and has relevance in understanding the role of metals in neurodegeneration.

Item Type: Journal Article
Publication: Neuroscience Letters
Publisher: Elsevier Ireland Ltd
Additional Information: Copyright of this article belongs to Elsevier Ireland Ltd.
Keywords: α-Synuclein;Copper;Iron;Electron microscopy;Fibrils;Parkinson's disease
Department/Centre: Division of Biological Sciences > Microbiology & Cell Biology
Date Deposited: 06 Nov 2007
Last Modified: 19 Sep 2010 04:41
URI: http://eprints.iisc.ac.in/id/eprint/12431

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