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- W2016322325 abstract "Fluorescein-labeled α- and β-octaarginine amides were synthesized. The route, by which these oligoarginine (OA) derivatives enter cells (hepatocytes, fibroblasts, macrophages), was investigated by confocal fluorescence microscopy. Comparisons (by co-localization experiments) with compounds of known penetration modes revealed that the β-octaarginine amide also uses multiple pathways to enter cells. There was no difference between the α- and the β-OAs. Like other cell-penetrating peptides (CPPs), the β-octaarginine eventually winds up in the nucleoli of the cell nuclei (cf. Chem. Biodiversity, 2004, 1, 65). Surprisingly, there was no entry of α- or β-OA into intact and healthy human erythrocytes (which do not possess a nucleus). Blood cells infected by Plasmodium falciparum (malaria parasite) were, however, entered readily, and the OAs went all the way through a couple of membranes into the parasite. The potential of these results for delivering specific antimalarial drugs directly into the parasite is discussed." @default.
- W2016322325 created "2016-06-24" @default.
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- W2016322325 date "2011-01-01" @default.
- W2016322325 modified "2023-10-16" @default.
- W2016322325 title "On the Mechanism of Eukaryotic Cell Penetration by α- and β-Oligoarginines - Targeting Infected Erythrocytes" @default.
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- W2016322325 doi "https://doi.org/10.1002/cbdv.201000318" @default.
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