The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.
Oligomers of the Arginine-rich Motif of the HIV-1 TAT Protein Are Capable of Transferring Plasmid DNA into Cells
Open accessAbstract
We constructed multimers of the TAT-(47-57) peptide. This polycationic peptide is known to be a protein and particle transduction domain and at the same time to comprise a nuclear localization function. Here we show that oligomers of the TAT-(47-57) peptide compact plasmid DNA to nanometric particles and stabilize DNA toward nuclease degradation. At optimized vector compositions, these peptides mediated gene delivery to cells in culture 6-8-fold more efficiently than poly-L-arginine or the mutant TAT(2)-M1. When DNA was precompacted with TAT peptides and polyethyleneimine (PEI), Superfect, or LipofectAMINE was added, transfection efficiency was enhanced up to 390-fold compared with the standard vectors. As early as after 4 h of transfection, reporter gene expression mediated by TAT-containing complexes was higher than the 24-h transfection level achieved with a standard PEI transfection. When cells were cell cycle-arrested by serum starvation or aphidicolin, TAT-mediated transfection was 3-fold more efficient than a standard PEI transfection in proliferating cells. In primary nasal epithelial cells and upon intratracheal instillation in vivo, TAT-containing complexes were superior to standard PEI vectors. These data together with confocal imaging of TAT-DNA complexes in cells support the hypothesis that the TAT nuclear localization sequence function is involved in enhancing gene transfer.
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Cites
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Cited by
Nonviral vectors for gene delivery
Mintzer, M. A., & Simanek, E. E. (2009) · Chemical Reviews · doi:10.1021/cr800409e · Cited by 2,366
Endosomal escape pathways for delivery of biologicals
Varkouhi, A. K., Scholte, M., Storm, G., & Haisma, H. J. (2011) · Journal of Controlled Release · doi:10.1016/j.jconrel.2010.11.004 · Cited by 1,561
Twenty years of cell‐penetrating peptides: from molecular mechanisms to therapeutics
Heitz, F., Morris, M. C., & Divita, G. (2009) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2009.00057.x · Cited by 867
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Tat peptide-mediated cellular delivery: back to basics
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Metadata
- Authors
- Rudolph, C., Plank, C., Lausier, J., Schillinger, U., Müller, R. H., & Rosenecker, J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-03
- Volume
- 278
- Issue
- 13
- Pages
- 11411-11418
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2056842925
- Cited by
- 275
- References
- 28
- FWCI
- 7.72
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Rudolph, C., Plank, C., Lausier, J., Schillinger, U., Müller, R. H., & Rosenecker, J. (2003). Oligomers of the Arginine-rich Motif of the HIV-1 TAT Protein Are Capable of Transferring Plasmid DNA into Cells. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m211891200
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