Author: Abes, Rachida; Moulton, Hong M.; Clair, Philippe; Yang, Sung-Tae; Abes, Said; Melikov, Kamran; Prevot, Paul; Youngblood, Derek S.; Iversen, Patrick L.; Chernomordik, Leonid V.; Lebleu, Bernard
Title: Delivery of steric block morpholino oligomers by (R-X-R)(4) peptides: structure–activity studies Document date: 2008_9_16
ID: 5j496cx0_1
Snippet: Protein transduction domains as penetratin or Tat 48-60 and synthetic cell penetrating peptides (CPP) as oligoarginine have generated a large interest for their seemingly unique mechanism of membrane translocation and for their capacity to transport various biomolecules across biological membranes (1) . Both assumptions have had to be re-visited since cellular uptake does involve endocytosis (2) and transport of biomolecules does not occur as eff.....
Document: Protein transduction domains as penetratin or Tat 48-60 and synthetic cell penetrating peptides (CPP) as oligoarginine have generated a large interest for their seemingly unique mechanism of membrane translocation and for their capacity to transport various biomolecules across biological membranes (1) . Both assumptions have had to be re-visited since cellular uptake does involve endocytosis (2) and transport of biomolecules does not occur as efficiently as anticipated at least at low concentrations. In a series of experiments carried out independently by several groups, CPPs mentioned above turned out inefficient in transporting uncharged splice correcting oligonucleotide (ON) analogs as peptide nucleic acids (PNA) or phosphorodiamidate morpholino oligomers (PMO) for a large part because CPP-conjugated material remained entrapped in endocytic vesicles (3) . Accordingly, peptides or drugs (such as chloroquine) leading to endosome destabilization did significantly increase splicing correction.
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