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Amyloid formation of the protein \u03b1-synuclein in brain cells is a hallmark of Parkinson\u2019s disease. \u03b1-Synuclein can bind several metal ions in vitro and such interactions may affect the assembly process. Here we used biophysical methods to study the effects of micromolar concentrations of Cu<jats:sup>2+<\/jats:sup> and Fe<jats:sup>3+<\/jats:sup> ions on amyloid formation of selected \u03b1-synuclein variants (wild-type and A53T \u03b1-synuclein, in normal and N-terminally acetylated forms). As shown previously, Cu<jats:sup>2+<\/jats:sup> speeds up aggregation of normal wild-type \u03b1-synuclein, but not the acetylated form. However, Cu<jats:sup>2+<\/jats:sup> has a minimal effect on (the faster) aggregation of normal A53T \u03b1-synuclein, despite that Cu<jats:sup>2+<\/jats:sup> binds to this variant. Like Cu<jats:sup>2+<\/jats:sup>, Fe<jats:sup>3+<\/jats:sup> speeds up aggregation of non-acetylated wild-type \u03b1-synuclein, but with acetylation, Fe<jats:sup>3+<\/jats:sup> instead slows down aggregation. In contrast, for A53T \u03b1-synuclein, regardless of acetylation, Fe<jats:sup>3+<\/jats:sup> slows down aggregation with the effect being most dramatic for acetylated A53T \u03b1-synuclein. The results presented here suggest a correlation between metal-ion modulation effect and intrinsic aggregation speed of the various \u03b1-synuclein variants.<\/jats:p>","DOI":"10.1007\/s10534-020-00234-4","type":"journal-article","created":{"date-parts":[[2020,3,13]],"date-time":"2020-03-13T11:03:06Z","timestamp":1584097386000},"page":"97-106","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":21,"title":["Differential effects of Cu2+ and Fe3+ ions on in vitro amyloid formation of biologically-relevant \u03b1-synuclein variants"],"prefix":"10.1007","volume":"33","author":[{"given":"Emma","family":"Lorentzon","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ranjeet","family":"Kumar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Istvan","family":"Horvath","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1058-1964","authenticated-orcid":false,"given":"Pernilla","family":"Wittung-Stafshede","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2020,3,13]]},"reference":[{"issue":"5","key":"234_CR1","doi-asserted-by":"publisher","first-page":"737","DOI":"10.1007\/s10534-018-0131-5","volume":"31","author":"J Aaseth","year":"2018","unstructured":"Aaseth J, Dusek P, Roos PM (2018) Prevention of progression in Parkinson's disease. 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