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Please use this identifier to cite or link to this item: http://apo.ansto.gov.au/dspace/handle/10238/2362

Title: Structure of dopamine induced α-synuclein oligomers.
Authors: Rekas, A
Knott, RB
Sokolova, A
Barnham, KJ
Perez, KA
Masters, CL
Drew, SC
Cappai, R
Curtain, CC
Pham, CLL
Keywords: Dopamine
EPR Spectrometers
Small Angle Scattering
Diseases
Agglomeration
Proteins
Issue Date: Sep-2010
Publisher: Springer
Citation: Rekas, A., Knott, R. B., Sokolova, A., Barnham, K. J., Perez, K. A., Masters, C. L., et al. (2010). Structure of dopamine induced α-synuclein oligomers. European Biophysics Journal, 39(10), 1407-1419.
Abstract: Inclusions of aggregated α-synuclein (α-syn) in dopaminergic neurons are a characteristic histological marker of Parkinson’s disease (PD). In vitro, α-syn in the presence of dopamine (DA) at physiological pH forms SDS-resistant non-amyloidogenic oligomers. We used a combination of biophysical techniques, including sedimentation velocity analysis, small angle X-ray scattering (SAXS) and circular dichroism spectroscopy to study the characteristics of α-syn oligomers formed in the presence of DA. Our SAXS data show that the trimers formed by the action of DA on α-syn consist of overlapping worm-like monomers, with no end-to-end associations. This lack of structure contrasts with the well-established, extensive β-sheet structure of the amyloid fibril form of the protein and its pre-fibrillar oligomers. We propose on the basis of these and earlier data that oxidation of the four methionine residues at the C- and N-terminal ends of α-syn molecules prevents their end-to-end association and stabilises oligomers formed by cross linking with DA-quinone/DA-melanin, which are formed as a result of the redox process, thus inhibiting formation of the β-sheet structure found in other pre-fibrillar forms of α-syn. © 2010, Springer. The original publication is available at www.springerlink.com
URI: http://dx.doi.org/10.1007/s00249-010-0595-x
http://apo.ansto.gov.au/dspace/handle/10238/2362
ISSN: 0175-7571
Appears in Collections:Journal Articles

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