Lipids and EGCG Affect α-Synuclein Association and Disruption of Nanodiscs.

ABSTRACT: Lipid membranes have recently been implicated in protein misfolding and disease etiology, including for α-synuclein and Parkinson's disease. However, studying the intersection of protein complex formation, membrane interactions, and bilayer disruption simultaneously is challenging. In particular, the efficacies of small molecule inhibitors for toxic protein aggregation are not well understood. Here, we used native mass spectrometry in combination with lipid nanodiscs to study α-synuclein-membrane interactions. α-Synuclein did not interact with zwitterionic 1,2-dimyristoyl-sn-glycero-3-phosphocholine lipids but interacted strongly with anionic 1,2-dimyristoyl-sn-glycero-3-phospho(1'-rac-glycerol) lipids, eventually leading to membrane disruption. Unsaturated 1-palmitoyl

SUBMITTER: Sanders HM 

PROVIDER: S-EPMC9202473 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature