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• W2047029292 abstract "We show that fluorine NMR can be used to monitor the insertion and change in conformation of a ¹⁹F-labeled cell-penetrating peptide upon interacting with the cellular plasma membrane. α-Synuclein and a construct comprising a cell-penetrating peptide covalently attached to its N-terminus were studied. Important information about the interaction of the proteins with CHO-K1 cells was obtained by monitoring the diminution of ¹⁹F resonances of 3-fluoro-l-tyrosine labeled proteins. For α-synuclein, a decrease in the resonance from position 39 was observed indicating that only the N-terminal third region of the protein interacts with plasma membrane. However, when the fusion construct was incubated with the cells, a decrease in the resonance from the fusion peptide region was noted with no change in the resonances from α-synuclein region. Longer incubation, studied by using confocal fluorescence microscopy, revealed that the fusion construct translocates into the cells, but α-synuclein alone did not cross the membrane in significant amounts." @default.
• W2047029292 created "2016-06-24" @default.
• W2047029292 creator A5047660543 @default.
• W2047029292 creator A5076371120 @default.
• W2047029292 date "2012-03-13" @default.
• W2047029292 modified "2023-09-27" @default.
• W2047029292 title "Interaction of α-Synuclein and a Cell Penetrating Fusion Peptide with Higher Eukaryotic Cell Membranes Assessed by ¹⁹F NMR" @default.
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• W2047029292 doi "https://doi.org/10.1021/mp200615m" @default.
• W2047029292 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3319258" @default.
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