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• W2000276790 abstract "The interaction of α-synuclein with phospholipid membranes has been examined using supported lipid bilayers and epi-fluorescence microscopy. The membranes contained phosphatidylcholine (PC) and phosphatidic acid (PA), which mix at physiological pH. Upon protein adsorption, the lipids undergo fluid−fluid phase separation into PC-rich and PA-rich regions. The protein preferentially adsorbs to the PA-rich regions. The adsorption and subsequent aggregation of α-synuclein was probed by tuning several parameters: the charge on the lipids, the charge on the protein, and the screening environment. Conditions which promoted the greatest extent of adsorption resulted in structurally heterogeneous aggregates, while comparatively homogeneous aggregates were observed under conditions whereby adsorption did not occur as readily. Our observation that different alterations to the system lead to different degrees of aggregation and different aggregate structures poses a challenge for drug discovery. Namely, therapies aimed at neutralizing α-synuclein must target a broad range of potentially toxic, membrane-bound assemblies." @default.
• W2000276790 created "2016-06-24" @default.
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• W2000276790 date "2010-02-26" @default.
• W2000276790 modified "2023-10-02" @default.
• W2000276790 title "Adsorption of α-Synuclein on Lipid Bilayers: Modulating the Structure and Stability of Protein Assemblies" @default.
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• W2000276790 doi "https://doi.org/10.1021/jp1006704" @default.
• W2000276790 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2855901" @default.
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