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- W2000712231 abstract "Gauging the interactions of a natively unfolded Parkinson disease-related protein, alpha-synuclein (α-syn) with membranes and its pathways between and within cells is important for understanding its pathogenesis. Here, to address these questions, we use a robust β-barrel channel, α-hemolysin, reconstituted into planar lipid bilayers. Transient, ∼95% blockage of the channel current by α-syn was observed when 1), α-syn was added from the membrane side where the shorter (stem) part of the channel is exposed; and 2), the applied potential was lower on the side of α-syn addition. While the on-rate of α-syn binding to the channel strongly increased with the applied field, the off-rate displayed a turnover behavior. Statistical analysis suggests that at voltages >50 mV, a significant fraction of the α-syn molecules bound to the channel undergoes subsequent translocation. The observed on-rate varied by >100 times depending on the bilayer lipid composition. Removal of the last 25 amino acids from the highly negatively charged C-terminal of α-syn resulted in a significant decrease in the binding rates. Taken together, these results demonstrate that β-barrel channels may serve as sensitive probes of α-syn interactions with membranes as well as model systems for studies of channel-assisted protein transport." @default.
- W2000712231 created "2016-06-24" @default.
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- W2000712231 date "2014-02-01" @default.
- W2000712231 modified "2023-09-27" @default.
- W2000712231 title "Alpha-Synuclein Lipid-Dependent Membrane Binding and Translocation through the α-Hemolysin Channel" @default.
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- W2000712231 doi "https://doi.org/10.1016/j.bpj.2013.12.028" @default.
- W2000712231 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3944825" @default.
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