Virus-sized self-assembling lamellar complexes between plasmid DNA and cationic micelles promote gene transfer
| Autor: | Gerardo Byk, Tsiala Boukhnikachvili, Christian Herviou, Jean-François Mayaux, Anne-Marie Lachagès, Bruno Pitard, Daniel Scherman, Marc Airiau, Joel Crouzet, Catherine Dubertret, Olivier Aguerre |
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| Rok vydání: | 1997 |
| Předmět: |
Multidisciplinary
Genetic Vectors Gene Transfer Techniques Supramolecular chemistry Biological Sciences Biology Micelle chemistry.chemical_compound Plasmid Biochemistry chemistry Viruses Calcium chloride transformation Polyamines Biophysics Lamellar structure DNA Circular Lipid bilayer Gene DNA Plasmids |
| Zdroj: | Proceedings of the National Academy of Sciences. 94:14412-14417 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.94.26.14412 |
| Popis: | Gene therapy is based on the vectorization of genes to target cells and their subsequent expression. Cationic amphiphile-mediated delivery of plasmid DNA is the nonviral gene transfer method most often used. We examined the supramolecular structure of lipopolyamine/plasmid DNA complexes under various condensing conditions. Plasmid DNA complexation with lipopolyamine micelles whose mean diameter was 5 nm revealed three domains, depending on the lipopolyamine/plasmid DNA ratio. These domains respectively corresponded to negatively, neutrally, and positively charged complexes. Transmission electron microscopy and x-ray scattering experiments on complexes originating from these three domains showed that although their morphology depends on the lipopolyamine/plasmid DNA ratio, their particle structure consists of ordered domains characterized by even spacing of 80 Å, irrespective of the lipid/DNA ratio. The most active lipopolyamine/DNA complexes for gene transfer were positively charged. They were characterized by fully condensed DNA inside spherical particles (diameter: 50 nm) sandwiched between lipid bilayers. These results show that supercoiled plasmid DNA is able to transform lipopolyamine micelles into a supramolecular organization characterized by ordered lamellar domains. |
| Databáze: | OpenAIRE |
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