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- W2077029463 abstract "As endocytic uptake of the Antennapedia homeodomain-derived penetratin peptide (RQIKIWFQNRRMKWKK) is finally being revealed, some of the early views about penetratin need to be reconsidered. Endocytic uptake seems to contradict the indispensability of tryptophans and also the minimum length of 16 amino acid residues for efficient internalization. To revise the membrane translocation of penetratin, two penetratin analogs were designed and synthesized: a peptide in which tryptophans were replaced by phenylalanines (Phe6, 14-penetratin, RQIKIFFQNRRMKFKK) and a shortened analog (dodeca-penetratin, RQIKIWF-R-KWKK) made up of only 12 residues. The peptides were fluorescently labeled and applied to live, unfixed cells from various lines. Cellular uptake was analysed by confocal microscopy and flow cytometry. Low temperature or ATP-depletion blocked the intracellular entry of all three penetratin peptides. A decrease in membrane fluidity or cholesterol depletion with methyl-β-cyclodextrin greatly inhibited peptide uptake, showing the involvement of cholesterol-rich lipid rafts in internalization. Exogenous heparan sulfate also diminished the internalization of penetratin and its derivatives, reflecting the paramount importance of electrostatic interactions with polyanionic cell-surface proteoglycans. The beneficial presence of tryptophans is supported by observations on the decreased cellular uptake of Phe6, 14-penetratin. The maintained translocational efficiency of dodeca-penetratin demonstrates that a thorough understanding of penetratin internalization can yield new penetratin analogs with unaltered translocational abilities. This study provides evidence on the energy-dependent and lipid raft-mediated endocytic uptake of penetratin and highlights the necessity of revealing those pathways that cationic cell-penetrating peptides employ to enter live cells. Copyright © 2005 European Peptide Society and John Wiley & Sons, Ltd." @default.
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- W2077029463 date "2005-01-01" @default.
- W2077029463 modified "2023-10-16" @default.
- W2077029463 title "Investigation of penetratin peptides. Part 2.In vitro uptake of penetratin and two of its derivatives" @default.
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- W2077029463 doi "https://doi.org/10.1002/psc.678" @default.
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