Unveiling a Selective Mechanism for the Inhibition of α-Synuclein Aggregation by β-Synuclein.

ABSTRACT: α-Synuclein (αS) is an intrinsically disordered protein that is associated with Parkinson's disease (PD) through its ability to self-assemble into oligomers and fibrils. Inhibition of this oligomerization cascade is an interesting approach to developing therapeutical strategies and β-synuclein (βS) has been described as a natural negative regulator of this process. However, the biological background and molecular mechanisms by which this inhibition occurs is unclear. Herein, we focused on assessing the effect of βS on the aggregation of five αS pathological mutants linked to early-onset PD (A30P, E46K, H50Q, G51D and A53T). By coupling single molecule fluorescence spectroscopy to a cell-free protein expression system, we validated the ability of βS to act as a chaperone of αS, effectively

SUBMITTER: Leitao A 

PROVIDER: S-EPMC5855556 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature