Histidine-rich peptides and polymers for nucleic acids delivery
Identifieur interne : 002274 ( Main/Exploration ); précédent : 002273; suivant : 002275Histidine-rich peptides and polymers for nucleic acids delivery
Auteurs : Chantal Pichon [France] ; Christine Gonçalves [France] ; Patrick Midoux [France]Source :
- Advanced Drug Delivery Reviews [ 0169-409X ] ; 2001.
English descriptors
- Teeft :
- Acad, Acidic, Acidic medium, Antisense, Biochemistry, Bioconjug, Biol, Biological activity, Cationic, Cationic polymers, Cell nucleus, Cell surface, Chem, Chloroquine, Complexed, Confocal microscope, Cytosol, Cytosolic, Cytosolic delivery, Destabilization, Drug delivery reviews, E5wyg, Egfp, Electrostatic interactions, Encoding, Endosomal membrane, Endosomes, Endothelial cells, Extracellular medium, Fusogenic, Fusogenic peptides, Gene, Gene delivery, Gene expression, Gene transfer, Glycosylated, Glycosylated polylysines, H5wyg, H5wyg peptide, Hela cells, Hepes, Hepes buffer, Hepg2, Hepg2 cells, Histidine, Histidyl, Histidyl residues, Histidylated, Histidylated oligolysine, Histidylated oligolysines, Histidylated polylysine, Histidylated polylysines, Imidazole, Imidazole protonation, Imidazole protonation mediates, Interpeptide bonds, Lactosylated, Lipid, Liposome, Luciferase, Luciferase activity, Melittin, Membrane, Membrane permeabilization, Midoux, Molar ratio, Molecular weight, Monsigny, Natl, Nuclear delivery, Nuclear import, Nuclear localization signal, Nuclear pores, Nucleic, Nucleic acids, Oligolysine, Oligonucleotides, Pcmvluc, Pdna, Pdna complexes, Pdna delivery, Peptide, Permeabilization, Phosphate buffer saline, Physiological salt concentration, Pichon, Plasma membrane, Plasmid, Polyethylenimine, Polyfection, Polylysine, Polylysine conjugate, Polylysines, Polymer, Polyplexes, Polyplexes stability, Positive charges, Proc, Propidium, Propidium iodide, Protonation, Qels measurements, Relative light units, Right target cells, Roche, Serum proteins, Transfecting cells, Transfection, Transmission electron microscopy, Unpackaging, Uorescence, Uorescence intensity, Vesicle.
Abstract
Abstract: Nucleic acids transfer into mammalian cells requires devices to improve their escape from endocytic vesicles where they are mainly confined following cellular uptake. In this review, we describe histidine-rich molecules that enable the transfer of plasmid and oligonucleotides (ODN) in human and non-human cultured cells. An histidine-rich peptide which permeabilizes biological membrane at pH 6.4, favored the transfection mediated by lactosylated polylysine/pDNA complexes. Histidylated polylysine forms cationic particles of 100 nm with a plasmid and yielded a transfection of 3–4.5 orders of magnitude higher than polylysine. The biological activity of antisense ODN was increased more than 20-fold when it was complexed with highly histidylated oligolysine into small cationic spherical particles of 35 nm. Evidence that imidazole protonation mediates the effect of these molecules in endosomes are provided. We also describe a disulfide-containing polylysine conjugate capable of mediating DNA unpackaging in a reductive medium and to increase the transfection efficiency. Overall, these molecules constitute interesting devices for developing non-viral gene delivery systems.
Url:
DOI: 10.1016/S0169-409X(01)00221-6
Affiliations:
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type="ISSN">0169-409X</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Acad</term><term>Acidic</term><term>Acidic medium</term><term>Antisense</term><term>Biochemistry</term><term>Bioconjug</term><term>Biol</term><term>Biological activity</term><term>Cationic</term><term>Cationic polymers</term><term>Cell nucleus</term><term>Cell surface</term><term>Chem</term><term>Chloroquine</term><term>Complexed</term><term>Confocal microscope</term><term>Cytosol</term><term>Cytosolic</term><term>Cytosolic delivery</term><term>Destabilization</term><term>Drug delivery reviews</term><term>E5wyg</term><term>Egfp</term><term>Electrostatic interactions</term><term>Encoding</term><term>Endosomal membrane</term><term>Endosomes</term><term>Endothelial cells</term><term>Extracellular medium</term><term>Fusogenic</term><term>Fusogenic peptides</term><term>Gene</term><term>Gene delivery</term><term>Gene expression</term><term>Gene transfer</term><term>Glycosylated</term><term>Glycosylated polylysines</term><term>H5wyg</term><term>H5wyg peptide</term><term>Hela cells</term><term>Hepes</term><term>Hepes buffer</term><term>Hepg2</term><term>Hepg2 cells</term><term>Histidine</term><term>Histidyl</term><term>Histidyl residues</term><term>Histidylated</term><term>Histidylated oligolysine</term><term>Histidylated oligolysines</term><term>Histidylated polylysine</term><term>Histidylated polylysines</term><term>Imidazole</term><term>Imidazole protonation</term><term>Imidazole protonation mediates</term><term>Interpeptide bonds</term><term>Lactosylated</term><term>Lipid</term><term>Liposome</term><term>Luciferase</term><term>Luciferase activity</term><term>Melittin</term><term>Membrane</term><term>Membrane permeabilization</term><term>Midoux</term><term>Molar ratio</term><term>Molecular weight</term><term>Monsigny</term><term>Natl</term><term>Nuclear delivery</term><term>Nuclear import</term><term>Nuclear localization 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microscopy</term><term>Unpackaging</term><term>Uorescence</term><term>Uorescence intensity</term><term>Vesicle</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Nucleic acids transfer into mammalian cells requires devices to improve their escape from endocytic vesicles where they are mainly confined following cellular uptake. In this review, we describe histidine-rich molecules that enable the transfer of plasmid and oligonucleotides (ODN) in human and non-human cultured cells. An histidine-rich peptide which permeabilizes biological membrane at pH 6.4, favored the transfection mediated by lactosylated polylysine/pDNA complexes. Histidylated polylysine forms cationic particles of 100 nm with a plasmid and yielded a transfection of 3–4.5 orders of magnitude higher than polylysine. The biological activity of antisense ODN was increased more than 20-fold when it was complexed with highly histidylated oligolysine into small cationic spherical particles of 35 nm. Evidence that imidazole protonation mediates the effect of these molecules in endosomes are provided. We also describe a disulfide-containing polylysine conjugate capable of mediating DNA unpackaging in a reductive medium and to increase the transfection efficiency. Overall, these molecules constitute interesting devices for developing non-viral gene delivery systems.</div></front></TEI><affiliations><list><country><li>France</li></country><region><li>Centre-Val de Loire</li><li>Région Centre</li></region><settlement><li>Orléans</li></settlement></list><tree><country name="France"><region name="Centre-Val de Loire"><name sortKey="Pichon, Chantal" sort="Pichon, Chantal" uniqKey="Pichon C" first="Chantal" last="Pichon">Chantal Pichon</name></region><name sortKey="Goncalves, Christine" sort="Goncalves, Christine" uniqKey="Goncalves C" first="Christine" last="Gonçalves">Christine Gonçalves</name><name sortKey="Midoux, Patrick" sort="Midoux, Patrick" uniqKey="Midoux P" first="Patrick" last="Midoux">Patrick Midoux</name><name sortKey="Midoux, Patrick" sort="Midoux, Patrick" uniqKey="Midoux P" first="Patrick" last="Midoux">Patrick Midoux</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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