Structure of dopamine induced α-synuclein oligomers

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dc.contributor.authorRekas, Aen_AU
dc.contributor.authorKnott, RBen_AU
dc.contributor.authorSokolova, AVen_AU
dc.contributor.authorBarnham, KJen_AU
dc.contributor.authorPerez, KAen_AU
dc.contributor.authorMasters, CLen_AU
dc.contributor.authorDrew, SCen_AU
dc.contributor.authorCappai, Ren_AU
dc.contributor.authorCurtain, CCen_AU
dc.contributor.authorPham, CLLen_AU
dc.date.accessioned2010-08-30T03:39:14Zen_AU
dc.date.available2010-08-30T03:39:14Zen_AU
dc.date.issued2010-3-23en_AU
dc.date.statistics2010-09en_AU
dc.description.abstractInclusions 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.en_AU
dc.identifier.citationRekas, A., Knott, R. B., Sokolova, A., Barnham, K. J., Perez, K. A., Masters, C. L., Drew, S. C., Cappai, R., Curtain, C. C., & Pham, C. L. L. (2010). Structure of dopamine induced α-synuclein oligomers. European Biophysics Journal, 39(10), 1407-1419. doi:10.1007/s00249-010-0595-xen_AU
dc.identifier.govdoc2542en_AU
dc.identifier.issn0175-7571en_AU
dc.identifier.issue10en_AU
dc.identifier.journaltitleEuropean Biophysics Journalen_AU
dc.identifier.pagination1407-1419en_AU
dc.identifier.urihttp://dx.doi.org/10.1007/s00249-010-0595-xen_AU
dc.identifier.urihttp://apo.ansto.gov.au/dspace/handle/10238/2362en_AU
dc.identifier.volume39en_AU
dc.language.isoenen_AU
dc.publisherSpringeren_AU
dc.subjectDopamineen_AU
dc.subjectEPR spectrometersen_AU
dc.subjectSmall angle scatteringen_AU
dc.subjectDiseasesen_AU
dc.subjectAgglomerationen_AU
dc.subjectProteinsen_AU
dc.titleStructure of dopamine induced α-synuclein oligomersen_AU
dc.typeJournal Articleen_AU
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