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

ABSTRACT: 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, desp

SUBMITTER: Lorentzon E 

PROVIDER: S-EPMC7295844 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature