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- W2607479327 abstract "Glycosaminoglycans (GAGs), which are covalently-linked membrane proteins at the cell surface have recently been suggested to involve in not only endocytic cellular uptake but also non-endocytic direct cell membrane translocation of arginine-rich cell-penetrating peptides (CPPs). However, in-situ comprehensive observation and the quantitative analysis of the direct membrane translocation processes are challenging, and the mechanism therefore remains still unresolved. In this work, real-time in-cell NMR spectroscopy was applied to investigate the direct membrane translocation of octaarginine (R8) into living cells. By introducing 4-trifluoromethyl-l-phenylalanine to the N terminus of R8, the non-endocytic membrane translocation of 19F-labeled R8 (19F-R8) into a human myeloid leukemia cell line was observed at 4 °C with a time resolution in the order of minutes. 19F NMR successfully detected real-time R8 translocation: the binding to anionic GAGs at the cell surface, followed by the penetration into the cell membrane, and the entry into cytosol across the membrane. The NMR concentration analysis enabled quantification of how much of R8 was staying in the respective translocation processes with time in situ. Taken together, our in-cell NMR results provide the physicochemical rationale for spontaneous penetration of CPPs in cell membranes." @default.
- W2607479327 created "2017-04-28" @default.
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- W2607479327 date "2017-04-15" @default.
- W2607479327 modified "2023-10-02" @default.
- W2607479327 title "Glycosaminoglycan Binding and Non-Endocytic Membrane Translocation of Cell-Permeable Octaarginine Monitored by Real-Time In-Cell NMR Spectroscopy" @default.
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- W2607479327 doi "https://doi.org/10.3390/ph10020042" @default.
- W2607479327 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5490399" @default.
- W2607479327 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28420127" @default.
- W2607479327 hasPublicationYear "2017" @default.
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