Abstract
Because α-Synuclein binds to anionic lipids and synaptic vesicles consist of 12% 18:0-22:6 phosphatidylserine (SDPS), we asked where this asymmetric lipid partitions, and how it affects α-Synuclein partitioning in a lipid raft system. Our coarse-grained molecular dynamics simulations of SDPS in a lipid raft composition show that 18:0-22:6 PS partitions to the liquid disordered phase (Ld). Additional simulations of lyso-18:0 and lyso-22:6 and subsequent energy fluctuations analysis demonstrate that SDPS partitioning to Ld is due to the 22:6 acyl-chain's greater affinity for Ld than the 18:0 chain's affinity for Lo. Furthermore, we show that α-synuclein's preference for anionic lipids drives it to join SDPS in the Ld phase. Knowing that the remainder of the synaptic vesicle composition is largely uncharged, we propose that SDPS will drive α-synuclein to Ld regions of the synaptic vesicle mixture.
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