Stable polyplexes based on arginine-containing oligopeptides for in vivo gene delivery.

Sonya Vasto, Sonya Vasto, Drijfhout, Vasto, Van'T Noordende, Van Rossenberg, Van Keulen, Biessen, Koerten, Van Berkel, Spies

Risultato della ricerca: Articlepeer review

28 Citazioni (Scopus)


In this study, we investigated to what extent the stability and transduction capacity of polyplexed DNA can be improved by optimizing the condensing peptide sequence. We have synthesized a small library of cationic peptides, at which the lysine/arginine ratio and the cation charge were varied. All peptides were able to compact DNA, at which polyplexes of short lysine-rich sequences were considerably larger than those of elongated or arginine-rich peptides (GM102 and GM202). In addition, the arginine-rich peptides GM102 and GM202 rendered the polyplexes resistant to plasma incubation or DNase I-mediated digestion. While all peptides were found to improve the transfection efficiency in HepG2 cells, only the GM102- and GM202-derived polyplexes could be specifically targeted to HepG2 cells by incorporation of a ligand-derivatized YKAK8WK peptide. We propose that GM102 and GM202 combine the advantage of small condensing peptides to give small-sized polyplexes with the superior stability of condensing polymers, which makes GM102 and GM202 excellent candidates for future in vivo gene therapy studies.
Lingua originaleEnglish
pagine (da-a)457-464
Numero di pagine8
RivistaGene Therapy
Stato di pubblicazionePublished - 2004

All Science Journal Classification (ASJC) codes

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