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Differential effects of Cu2+ and Fe3+ ions on in vitro amyloid formation of biologically-relevant α-synuclein variants.

Artikel i vetenskaplig tidskrift
Författare Emma Lorentzon
Ranjeet Kumar
Istvan Horvath
Pernilla Wittung-Stafshede
Publicerad i Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine
Volym 33
Nummer/häfte 97-106
ISSN 1572-8773
Publiceringsår 2020
Publicerad vid Institutionen för kemi och molekylärbiologi
Språk en
Länkar dx.doi.org/10.1007/s10534-020-00234...
www.ncbi.nlm.nih.gov/entrez/query.f...
Ämnesord Acetylation; Amyloid formation; Metal ions; Parkinson’s disease; Thioflavin T; α-Synuclein
Ämneskategorier Molekylärbiologi

Sammanfattning

Alterations in metal ion homeostasis appear coupled to neurodegenerative disorders but mechanisms are unknown. Amyloid formation of the protein α-synuclein in brain cells is a hallmark of Parkinson's disease. α-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 Cu2+ and Fe3+ ions on amyloid formation of selected α-synuclein variants (wild-type and A53T α-synuclein, in normal and N-terminally acetylated forms). As shown previously, Cu2+ speeds up aggregation of normal wild-type α-synuclein, but not the acetylated form. However, Cu2+ has a minimal effect on (the faster) aggregation of normal A53T α-synuclein, despite that Cu2+ binds to this variant. Like Cu2+, Fe3+ speeds up aggregation of non-acetylated wild-type α-synuclein, but with acetylation, Fe3+ instead slows down aggregation. In contrast, for A53T α-synuclein, regardless of acetylation, Fe3+ slows down aggregation with the effect being most dramatic for acetylated A53T α-synuclein. The results presented here suggest a correlation between metal-ion modulation effect and intrinsic aggregation speed of the various α-synuclein variants.

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