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  • 1.
    EL Andaloussi, Samir
    et al.
    Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för neurokemi.
    Johansson, Henrik
    Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för neurokemi.
    Holm, Tina
    Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för neurokemi.
    Langel, Ülo
    Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för neurokemi.
    A novel cell-penetrating peptide, M918, for efficient delivery of proteins and peptide nucleic acids2007Inngår i: Molecular Therapy, ISSN 1525-0016, E-ISSN 1525-0024, Vol. 15, nr 10, s. 1820-1826Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    Cell-penetrating peptides (CPPs) have attracted increasing attention in the past decade as a result of their high potential to convey various, otherwise impermeable, bioactive agents across cellular plasma membranes. Albeit different CPPs have proven potent in delivery of different cargoes, there is generally a correlation between high efficacy and cytotoxicity for these peptides. Hence, it is of great importance to find new, non-toxic CPPs with more widespread delivery properties. We present a novel CPP, M918, that efficiently translocates various cells in a non-toxic fashion. In line with most other CPPs, the peptide is internalized mainly via endocytosis, and in particular macropinocytosis, but independent of glycosaminoglycans on the cell surface. In addition, in a splice correction assay using antisense peptide nucleic acid (PNA) conjugated via a disulphide bridge to M918 (M918-PNA), we observed a dose-dependent increase in correct splicing, exceeding the effect of other CPPs. Our data demonstrate that M918 is a novel CPP that can be used to translocate different cargoes inside various cells efficiently.

  • 2.
    Johansson, Henrik
    et al.
    Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för neurokemi.
    El-Andaloussi, Samir
    Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för neurokemi.
    Holm, Tina
    Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för neurokemi.
    Mäe, Maarja
    Jaak, Jänes
    Maimets, Toivo
    Langel, Ülo
    Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för neurokemi.
    Characterization of a novel cytotoxic cell-penetrating peptide derived from p14ARF protein2008Inngår i: Molecular Therapy, ISSN 1525-0016, E-ISSN 1525-0024, Vol. 16, nr 1, s. 115-123Artikkel i tidsskrift (Fagfellevurdert)
  • 3.
    Lehto, Taavi
    et al.
    Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för neurokemi.
    Simonson, Oscar E.
    Mäger, Imre
    Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för neurokemi.
    Ezzat, Kariem
    Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för neurokemi.
    Sork, Helena
    Copolovici, Dana-Maria
    Viola, Joana R.
    Zaghloul, Eman M.
    Lundin, Per
    Moreno, Pedro M. D.
    Mäe, Maarja
    Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för neurokemi.
    Oskolkov, Nikita
    Suhorutšenko, Julia
    Smith, C. I. Edvard
    EL Andaloussi, Samir
    A Peptide-based Vector for Efficient Gene Transfer In Vitro and In Vivo2011Inngår i: Molecular Therapy, ISSN 1525-0016, E-ISSN 1525-0024, Vol. 19, nr 8, s. 1457-1467Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    Finding suitable nonviral delivery vehicles for nucleic acid-based therapeutics is a landmark goal in gene therapy. Cell-penetrating peptides (CPPs) are one class of delivery vectors that has been exploited for this purpose. However, since CPPs use endocytosis to enter cells, a large fraction of peptides remain trapped in endosomes. We have previously reported that stearylation of amphipathic CPPs, such as transportan 10 (TP10), dramatically increases transfection of oligonucleotides in vitro partially by promoting endosomal escape. Therefore, we aimed to evaluate whether stearyl-TP10 could be used for the delivery of plasmids as well. Our results demonstrate that stearyl-TP10 forms stable nanoparticles with plasmids that efficiently enter different cell-types in a ubiquitous manner, including primary cells, resulting in significantly higher gene expression levels than when using stearyl-Arg9 or unmodified CPPs. In fact, the transfection efficacy of stearyl-TP10 almost reached the levels of Lipofectamine 2000 (LF2000), however, without any of the observed lipofection-associated toxicities. Most importantly, stearyl-TP10/plasmid nanoparticles are nonimmunogenic, mediate efficient gene delivery in vivo, when administrated intramuscularly (i.m.) or intradermally (i.d.) without any associated toxicity in mice.

  • 4. Nikravesh, Abbas
    et al.
    Dryselius, Rikard
    Faridani, Omid R
    Goh, Shan
    Sadeghizadeh, Majid
    Behmanesh, Mehrdad
    Ganyu, Anita
    Klok, Erik Jan
    Zain, Rula
    Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för molekylärbiologi och funktionsgenomik.
    Good, Liam
    Antisense PNA Accumulates in Escheria coli and mediates a Long Post-antibiotic Effect2008Inngår i: Molecular Therapy, ISSN 1525-0016, E-ISSN 1525-0024, Vol. 15, nr 8, s. 1537-1542Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    Antisense agents that target growth-essential genes display surprisingly potent bactericidal properties. In particular, peptide nucleic acid (PNA) and phosphorodiamidate morpholino oligomers linked to cationic carrier peptides are effective in time kill assays and as inhibitors of bacterial peritonitis in mice. It is unclear how these relatively large antimicrobials overcome stringent bacterial barriers and mediate killing. Here we determined the transit kinetics of peptide–PNAs and observed an accumulation of cell-associated PNA in Escherichia coli and slow efflux. An inhibitor of drug efflux pumps did not alter peptide–PNA potency, indicating a lack of active efflux from cells. Consistent with cell retention, the post-antibiotic effect (PAE) of the anti-acyl carrier protein (acpP) peptide–PNA was greater than 11 hours. Bacterial cell accumulation and a long PAE are properties of significant interest for antimicrobial development.

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