The reduction of the positive charges of polylysine by partial gluconoylation increases the transfection efficiency of polylysine/DNA complexes
Identifieur interne : 002896 ( Main/Merge ); précédent : 002895; suivant : 002897The reduction of the positive charges of polylysine by partial gluconoylation increases the transfection efficiency of polylysine/DNA complexes
Auteurs : Patrick Erbacher [France] ; Annie Claude Roche [France] ; Michel Monsigny [France] ; Patrick Midoux [France]Source :
- Biochimica et Biophysica Acta:Biomembranes [ 0005-2736 ] ; 1997-02.
Abstract
A polylysine partially substituted with polyhydroxyalkanoyl residues and specially with gluconoyl residues was developed in order to increase the transfection efficiency by decreasing the strength of the electrostatic interactions between the DNA and the cationic polymer. Partially gluconoylated polylysine/DNA complexes were more easily dissociated in solution and their transfection efficiency in the presence of chloroquine, evaluated with HepG2 cells, a human hepatocarcinoma line, was higher when 43 +/- 4% of the epsilon-amino groups of polylysine were blocked with gluconoyl residues. Partially gluconoylated polylysine/plasmid complexes were efficient in transfecting different adherent as well as non-adherent cell lines. Partially gluconoylated polylysine formed highly soluble (above 100 micrograms/ml in DNA) complexes with DNA plasmids. In addition, partially gluconoylated polylysine bearing few lactosyl residues increased the transfection efficiency of HepG2 cells which express a galactose-specific membrane lectin.
Url:
DOI: 10.1016/s0005-2736(96)00204-0
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<country>France</country>
<placeName><settlement type="city">Orléans</settlement>
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<region type="region" nuts="2">Centre-Val de Loire</region>
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<orgName type="university">Université d'Orléans</orgName>
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<author><name sortKey="Midoux, Patrick" sort="Midoux, Patrick" uniqKey="Midoux P" first="Patrick" last="Midoux">Patrick Midoux</name>
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<orgName>Centre de biophysique moléculaire</orgName>
<orgName type="acronym">CBM</orgName>
<date type="start">1967-01-01</date>
<desc> <address> <addrLine>Rue Charles Sadron 45071 ORLEANS CEDEX 2</addrLine>
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<orgName>Université d'Orléans</orgName>
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<desc> <address> <addrLine>Château de la Source - Avenue du Parc Floral - BP 6749 - 45067 Orléans cedex 2</addrLine>
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<orgName>Institut National de la Santé et de la Recherche Médicale</orgName>
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<desc> <address> <addrLine>101, rue de Tolbiac, 75013 Paris </addrLine>
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</address>
<ref type="url">http://www.inserm.fr</ref>
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<tutelle name="UPR4301" active="#struct-441569" type="direct"><org type="institution" xml:id="struct-441569" status="VALID"> <idno type="IdRef">02636817X</idno>
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<orgName>Centre National de la Recherche Scientifique</orgName>
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<country>France</country>
<placeName><settlement type="city">Orléans</settlement>
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<idno type="DOI">10.1016/s0005-2736(96)00204-0</idno>
<series><title level="j">Biochimica et Biophysica Acta:Biomembranes</title>
<idno type="ISSN">0005-2736</idno>
<imprint><date type="datePub">1997-02</date>
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<front><div type="abstract" xml:lang="en"> <p>A polylysine partially substituted with polyhydroxyalkanoyl residues and specially with gluconoyl residues was developed in order to increase the transfection efficiency by decreasing the strength of the electrostatic interactions between the DNA and the cationic polymer. Partially gluconoylated polylysine/DNA complexes were more easily dissociated in solution and their transfection efficiency in the presence of chloroquine, evaluated with HepG2 cells, a human hepatocarcinoma line, was higher when 43 +/- 4% of the epsilon-amino groups of polylysine were blocked with gluconoyl residues. Partially gluconoylated polylysine/plasmid complexes were efficient in transfecting different adherent as well as non-adherent cell lines. Partially gluconoylated polylysine formed highly soluble (above 100 micrograms/ml in DNA) complexes with DNA plasmids. In addition, partially gluconoylated polylysine bearing few lactosyl residues increased the transfection efficiency of HepG2 cells which express a galactose-specific membrane lectin.</p>
</div>
</front>
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