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Sahin, Cagla; Østerlund, Eva Christina; Österlund, Nicklas; Costeira-Paulo, Joana; Pedersen, Jannik Nedergaard; Christiansen, Gunna; Nielsen, Janni; Grønnemose, Anne Louise; Amstrup, Søren Kirk; Tiwari, Manish K.; Rao, R. Shyama Prasad; Bjerrum, Morten Jannik; Ilag, Leopold L.; Davies, Michael J.; Marklund, Erik; Pedersen, Jan Skov; Landreh, Michael; Møller, Ian Max; Jørgensen, Thomas J. D.; Otzen, Daniel Erik
Journal of the American Chemical Society, 2022, Letnik: 144, Številka: 27Journal Article
α-Synuclein (α-Syn) is an intrinsically disordered protein which self-assembles into highly organized β-sheet structures that accumulate in plaques in brains of Parkinsonâs disease patients. Oxidative stress influences α-Syn structure and self-assembly; however, the basis for this remains unclear. Here we characterize the chemical and physical effects of mild oxidation on monomeric α-Syn and its aggregation. Using a combination of biophysical methods, small-angle X-ray scattering, and native ion mobility mass spectrometry, we find that oxidation leads to formation of intramolecular dityrosine cross-linkages and a compaction of the α-Syn monomer by a factor of â2. Oxidation-induced compaction is shown to inhibit ordered self-assembly and amyloid formation by steric hindrance, suggesting an important role of mild oxidation in preventing amyloid formation.
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JCR | SNIP | JCR | SNIP | JCR | SNIP | JCR | SNIP |
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in: SICRIS
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