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Peptide nanoparticle delivery of charge-neutral splice-switching morpholino oligonucleotides.
Medical Research Council , Laboratory of Molecular Biology, Cambridge Biomedical Campus, Cambridge, United Kingdom.
Department of Laboratory Medicine, Karolinska Institute, Karolinska University Hospital, Huddinge, Sweden.
Medical Research Council, Laboratory of Molecular Biology, Cambridge Biomedical Campus, Cambridge, United Kingdom.
Medical Research Council, Laboratory of Molecular Biology, Cambridge Biomedical Campus, Cambridge, United Kingdom.
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2015 (engelsk)Inngår i: Nucleic Acid Therapeutics, ISSN 2159-3337, E-ISSN 2159-3345, Vol. 25, nr 2, s. 65-77Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Oligonucleotide analogs have provided novel therapeutics targeting various disorders. However, their poor cellular uptake remains a major obstacle for their clinical development. Negatively charged oligonucleotides, such as 2'-O-Methyl RNA and locked nucleic acids have in recent years been delivered successfully into cells through complex formation with cationic polymers, peptides, liposomes, or similar nanoparticle delivery systems. However, due to the lack of electrostatic interactions, this promising delivery method has been unsuccessful to date using charge-neutral oligonucleotide analogs. We show here that lipid-functionalized cell-penetrating peptides can be efficiently exploited for cellular transfection of the charge-neutral oligonucleotide analog phosphorodiamidate morpholino. The lipopeptides form complexes with splice-switching phosphorodiamidate morpholino oligonucleotide and can be delivered into clinically relevant cell lines that are otherwise difficult to transfect while retaining biological activity. To our knowledge, this is the first study to show delivery through complex formation of biologically active charge-neutral oligonucleotides by cationic peptides.

sted, utgiver, år, opplag, sider
2015. Vol. 25, nr 2, s. 65-77
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Identifikatorer
URN: urn:nbn:se:su:diva-124913DOI: 10.1089/nat.2014.0511ISI: 000351833000002PubMedID: 25594433OAI: oai:DiVA.org:su-124913DiVA, id: diva2:891232
Tilgjengelig fra: 2016-01-06 Laget: 2016-01-06 Sist oppdatert: 2017-12-01bibliografisk kontrollert

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