Table 1.

Summary of PD-related point mutations of α-syn and their effects on its binding capacity to membranes.

Mutation	Effects on Lipid Membranes	Ref.
V15A	decreased affinity to phospholipids accompanied by an increased aggregation and seeding activity	[132]
A18T	less toxic than wildtype α-syn altered triglycerides reduce α-syn toxicity	[133]
A29S	less toxic than wildtype α-syn altered triglycerides decrease α-syn toxicity enhanced acetylation or SUMOylation are protective against α-syn toxicity	[133]
A30P	reduced binding to membranes formation of metal ion-induced pathologic oligomers was increased fibril formation is slower in A30P mutants compared to wildtype interaction of α-syn with lipid rafts is hindered	[85,134,135,136]
E46K	increased lipid interactions and disrupted membrane selectivity increased N-to-C interactions and coil compactness in the structure of lipid-unbound α-syn conformation of α-syn is altered upon interaction with a curved lipid bilayer	[137,138]
H50Q	enhances α-syn aggregation and toxicity without affecting the binding capacity to lipid membranes	[139]
G51D	decreased binding to lipid membrane fibril formation was accelerated	[136]
A53E	α-syn exhibits a low lipid binding capacity compared to wildtype	[140]
A53T	does not change the binding capacity of α-syn to membranes formation of metal ion-induced pathologic oligomers and fibril formation are increased α-syn monomers cause membrane thinning and facilitate the interaction with artificial lipid rafts iron-mediated oligomers do not impair the membrane, but facilitate the interaction with artificial lipid rafts no effect on the interaction of α-syn with lipid rafts	[85,136,141,142]
A53V	low binding affinity to membranes compared to wildtype less toxic than wildtype α-syn altered triglycerides reduce α-syn toxicity enhanced acetylation or SUMOylation are protective against α-syn toxicity	[133,140]