Investigating 14-3-3’s Binding Site upon Interaction with α-Synuclein Through Microscale Thermophoresis Based Competitive Assay

Parkinson’s Disease (PD) is a neurodegenerative disease characterized by the aggregation of α-synuclein to form toxic multimers in the neuronal cells of the body and brain. It has been shown that the 14-3-3 protein family influences the aggregation of α-synuclein by binding its multimers, preventing misfolding and delaying aggregation. This insight forms opportunities for potential therapeutic approaches regarding the pathogenesis of PD. Here, we performed a competitive assay based on microscale thermophoresis and show that 14-3-3’s amphipatic binding pocket may potentially be involved in the interaction between α-synuclein multimers and 14-3-3 proteins.