|
Home |
| Browse | |
|
|
Communities & Collections |
|
|
Issue Date |
|
|
Author |
|
|
Title |
|
|
Subject |
| Sign on to: | |
|
|
Receive email updates |
|
|
My APO authorized users |
|
|
Edit Profile |
|
|
|
|
|
About DSpace |
ANSTO Publications Online >
Journal Publications >
Journal Articles >
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 |
Files in This Item: There are no files associated with this item. |
Items in APO are protected by copyright, with all rights reserved, unless otherwise indicated.
|
DSpace Software Copyright © 2002-2010 Duraspace - Feedback |