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α-Synuclein-Induced Membrane Remodeling Is Driven by Binding Affinity, Partition Depth, and Interleaflet Order Asymmetry

[Image: see text] We have investigated the membrane remodeling capacity of the N-terminal membrane-binding domain of α-synuclein (α-Syn(100)). Using fluorescence correlation spectroscopy and vesicle clearance assays, we show that α-Syn(100) fully tubulates POPG vesicles, the first demonstration that...

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Main Authors: Braun, Anthony R., Lacy, Michael M., Ducas, Vanessa C., Rhoades, Elizabeth, Sachs, Jonathan N.
Formáid: Artigo
Teanga:Inglês
Foilsithe: American Chemical Society 2014
Rochtain Ar Líne:https://ncbi.nlm.nih.gov/pmc/articles/PMC4105054/
https://ncbi.nlm.nih.gov/pubmed/24960410
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/ja5016958
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