| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10797864 | Biochimica et Biophysica Acta (BBA) - Biomembranes | 2011 | 8 Pages |
Abstract
⺠Affinity of penetratin variants for plasma membrane vesicles (PMVs) was examined. ⺠Binding to PMVs is arginine-dependent and correlates with uptake in live cells. ⺠PMVs have a membrane composition representative of the cells they were derived from. ⺠The results suggest that membrane affinity is a key property for an efficient CPP.
Keywords
CPPFITCHEPESFM4-64DTTPenetratinCHO-K1PMvHBS4-(2-hydroxyethyl)-1-piperazineethanesulfonic acidHEPES-buffered salineArginineMembrane affinitydithiothreitolplasma membrane vesiclePlasma membrane vesiclesFormaldehydefluorescein isothiocyanateLysineCell-penetrating peptidecarboxyfluoresceinGABAgamma-amino-butyric acid
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Authors
Helene L. Ã
mand, Carolina L. Boström, Per Lincoln, Bengt Nordén, Elin K. Esbjörner,