Parkinson's Disease-associated mutations in α-synuclein alters its lipid-bound state

In this report, we use a tryptophan fluorescence assay to measure the binding of the α-helices of these PD-associated mutants to lipid membranes within the lipid depletion regime. We characterize the binding behavior of each helix, revealing that generally, the PD-associated mutants shift the equilibrium bound state away from the N-terminal helix of the protein toward Helix 2 at lower lipid concentrations. Altogether, our results indicate that disruption to the equilibrium binding of the two α-helices of α-synuclein could play a role in PD progression.PMID:38702883 | DOI:10.1016/j.bpj.2024.05.002
Source: Biophysical Journal - Category: Physics Authors: Source Type: research