A powerful cooperative interaction between a fusogenic peptide and lipofectamine for the enhancement of receptor‐targeted, non‐viral gene delivery via integrin receptors
Identifieur interne : 002422 ( Main/Exploration ); précédent : 002421; suivant : 002423A powerful cooperative interaction between a fusogenic peptide and lipofectamine for the enhancement of receptor‐targeted, non‐viral gene delivery via integrin receptors
Auteurs : Xiaohong Zhang [Royaume-Uni] ; Louise Collins [Royaume-Uni] ; John W. Fabre [Royaume-Uni]Source :
- The Journal of Gene Medicine [ 1099-498X ] ; 2001-11.
English descriptors
- Teeft :
- Amino, Amino acids, Cationic, Cationic lipids, Chloroquine, College hospital, Competitive binding, Control peptide, Cooperative interaction, Copyright, Culture medium, Dose studies, Endocytic, Endocytic vesicles, Fetal calf serum, Fuso, Fuso lipo, Fusogenic, Fusogenic peptide, Gene, Gene delivery, Gene therapy, Gene transfer, Hepg2, Hepg2 cell line, Hepg2 cells, Huh7, Huh7 cell line, John wiley sons, Lipo, Lipofectamine, Lipofectamine fusogenic peptide ratio, Nacl, Optimal concentrations, Peptide, Pgl2 plasmid, Pgl3 plasmid, Plasmid, Polylysinemolossin, Reporter gene, Room temperature, Surface charge, Transfected, Transfection, Transplantation, Vesicle, Zhang.
Abstract
Background: Following receptor‐mediated endocytosis, vector/DNA complexes require assistance to exit endocytic vesicles in order to avoid degradation in the lysosomes. Overcoming this barrier is a major challenge for the development of receptor‐targeted, non‐viral gene delivery. Methods: The fusogenic peptide of influenza virus haemagglutinin, lipofectamine and chloroquine were tested singly and in combination in various doses for promoting in vitro gene transfer by an integrin‐targeted, non‐viral DNA vector (polylysine‐molossin). Results: The fusogenic peptide and lipofectamine both individually promoted integrin‐targeted gene delivery. However, the combined use of these agents was particularly effective, even at concentrations where neither agent singly had any effect on promoting gene delivery by polylysine‐molossin. This optimal combination was effective on several cell lines and primary cell cultures. On the HuH7 cell line, it was ∼five‐fold more effective than optimal chloroquine concentrations for integrin‐targeted gene delivery and four to five times more effective than commercially available polyethylenimine. With the β‐galactosidase reporter gene, 60–65% of HepG2 cells and 75–80% of HuH7 cells were positive. The surface charge of polylysine‐molossin/DNA/lipofectamine/fusogenic peptide complexes was approximately the same as that of polylysine‐molossin/DNA complexes. The size distribution of the complexes suggested that competitive binding of polylysine‐molossin and lipofectamine to DNA influenced the overall efficacy of this approach. Conclusions: Although the mechanisms are not clear, the combined use of very low doses of two membrane‐destabilizing agents results in high levels of receptor‐targeted gene delivery. Copyright © 2001 John Wiley & Sons, Ltd.
Url:
DOI: 10.1002/jgm.224
Affiliations:
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Fabre</name><affiliation wicri:level="1"><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Department of Clinical Sciences, Institute of Liver Studies, King's College Hospital, Guy's, King's and St Thomas' School of Medicine, Bessemer Road, London SE5 9PJ</wicri:regionArea><wicri:noRegion>London SE5 9PJ</wicri:noRegion></affiliation><affiliation wicri:level="1"><country wicri:rule="url">Royaume-Uni</country></affiliation><affiliation wicri:level="1"><country xml:lang="fr" wicri:curation="lc">Royaume-Uni</country><wicri:regionArea>Correspondence address: Department of Clinical Sciences, Institute of Liver Studies, King's College Hospital, Bessemer Road, London SE5 9PJ</wicri:regionArea><wicri:noRegion>London SE5 9PJ</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">The Journal of Gene Medicine</title><title level="j" type="alt">JOURNAL OF GENE MEDICINE, THE</title><idno type="ISSN">1099-498X</idno><idno type="eISSN">1521-2254</idno><imprint><biblScope unit="vol">3</biblScope><biblScope unit="issue">6</biblScope><biblScope unit="page" from="560">560</biblScope><biblScope unit="page" to="568">568</biblScope><biblScope unit="page-count">9</biblScope><publisher>John Wiley & Sons, Ltd.</publisher><pubPlace>Chichester, UK</pubPlace><date type="published" when="2001-11">2001-11</date></imprint><idno type="ISSN">1099-498X</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">1099-498X</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Amino</term><term>Amino acids</term><term>Cationic</term><term>Cationic lipids</term><term>Chloroquine</term><term>College hospital</term><term>Competitive binding</term><term>Control peptide</term><term>Cooperative interaction</term><term>Copyright</term><term>Culture medium</term><term>Dose studies</term><term>Endocytic</term><term>Endocytic vesicles</term><term>Fetal calf serum</term><term>Fuso</term><term>Fuso lipo</term><term>Fusogenic</term><term>Fusogenic peptide</term><term>Gene</term><term>Gene delivery</term><term>Gene therapy</term><term>Gene transfer</term><term>Hepg2</term><term>Hepg2 cell line</term><term>Hepg2 cells</term><term>Huh7</term><term>Huh7 cell line</term><term>John wiley sons</term><term>Lipo</term><term>Lipofectamine</term><term>Lipofectamine fusogenic peptide ratio</term><term>Nacl</term><term>Optimal concentrations</term><term>Peptide</term><term>Pgl2 plasmid</term><term>Pgl3 plasmid</term><term>Plasmid</term><term>Polylysinemolossin</term><term>Reporter gene</term><term>Room temperature</term><term>Surface charge</term><term>Transfected</term><term>Transfection</term><term>Transplantation</term><term>Vesicle</term><term>Zhang</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Background: Following receptor‐mediated endocytosis, vector/DNA complexes require assistance to exit endocytic vesicles in order to avoid degradation in the lysosomes. Overcoming this barrier is a major challenge for the development of receptor‐targeted, non‐viral gene delivery. Methods: The fusogenic peptide of influenza virus haemagglutinin, lipofectamine and chloroquine were tested singly and in combination in various doses for promoting in vitro gene transfer by an integrin‐targeted, non‐viral DNA vector (polylysine‐molossin). Results: The fusogenic peptide and lipofectamine both individually promoted integrin‐targeted gene delivery. However, the combined use of these agents was particularly effective, even at concentrations where neither agent singly had any effect on promoting gene delivery by polylysine‐molossin. This optimal combination was effective on several cell lines and primary cell cultures. On the HuH7 cell line, it was ∼five‐fold more effective than optimal chloroquine concentrations for integrin‐targeted gene delivery and four to five times more effective than commercially available polyethylenimine. With the β‐galactosidase reporter gene, 60–65% of HepG2 cells and 75–80% of HuH7 cells were positive. The surface charge of polylysine‐molossin/DNA/lipofectamine/fusogenic peptide complexes was approximately the same as that of polylysine‐molossin/DNA complexes. The size distribution of the complexes suggested that competitive binding of polylysine‐molossin and lipofectamine to DNA influenced the overall efficacy of this approach. Conclusions: Although the mechanisms are not clear, the combined use of very low doses of two membrane‐destabilizing agents results in high levels of receptor‐targeted gene delivery. Copyright © 2001 John Wiley & Sons, Ltd.</div></front></TEI><affiliations><list><country><li>Royaume-Uni</li></country></list><tree><country name="Royaume-Uni"><noRegion><name sortKey="Zhang, Xiaohong" sort="Zhang, Xiaohong" uniqKey="Zhang X" first="Xiaohong" last="Zhang">Xiaohong Zhang</name></noRegion><name sortKey="Collins, Louise" sort="Collins, Louise" uniqKey="Collins L" first="Louise" last="Collins">Louise Collins</name><name sortKey="Fabre, John W" sort="Fabre, John W" uniqKey="Fabre J" first="John W." last="Fabre">John W. Fabre</name><name sortKey="Fabre, John W" sort="Fabre, John W" uniqKey="Fabre J" first="John W." last="Fabre">John W. Fabre</name><name sortKey="Fabre, John W" sort="Fabre, John W" uniqKey="Fabre J" first="John W." last="Fabre">John W. Fabre</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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