Histidine Containing Peptides and Polypeptides as Nucleic Acid Vectors
Identifieur interne : 000F90 ( Istex/Corpus ); précédent : 000F89; suivant : 000F91Histidine Containing Peptides and Polypeptides as Nucleic Acid Vectors
Auteurs : Patrick Midoux ; Eric Lecam ; Dominique Coulaud ; Etienne Delain ; Chantal PichonSource :
- Somatic Cell and Molecular Genetics [ 0740-7750 ] ; 2002-11-01.
Abstract
Abstract: Nucleic acid transfer in mammalian cells is drastically improved with devices which increase their delivery in the cytosol upon endocytosis. In this chapter, we describe the effect on plasmid DNA (pDNA) and oligonucleotide (ODN) transfer, of an histidine-rich peptide (H5WYG), histidylated oligolysine (HoK), and histidylated polylysine (HpK) designed on the basis of the membrane destabilization capacity of poly-L-histidine at a pH close to that of the endosomes. We report that H5WYG, which permeabilizes the cell membrane at pH 6.4, favors the transfection mediated by lactosylated polylysine/pDNA complexes and, by lowering the pH of extracellular medium, allows the loading of the cytosol and the cell nucleus with ODN. We show that HoK forms small cationic spherical particles of 35 nm with ODN and HpK rod or toroid cationic particles of 100 nm with pDNA. PEGylation stabilizes these particles at physiological salt concentration. We also show that (i) HoK/ODN complexes yield a more than 20-fold increase of the biological activity of antisense ODN towards the inhibition of transient as well as constitutive gene expression and (ii) HpK/pDNA complexes yield a transfection efficiency of 3–4.5 order of magnitude higher than do polylysine/pDNA complexes. We also provide evidence that the effect of these polyhistidylated molecules is mediated by imidazole protonation in endosomes. Overall our data show that polyhistidylated molecules constitute interesting devices for an efficient cytosolic delivery of nucleic acids, and that ionic complexes between histidylated polylysine and a pDNA are attractive for developing a nonviral gene delivery system.
Url:
DOI: 10.1023/A:1022931923153
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ISTEX:09F94AE257E55C800B44108232926C0C6411CA96Le document en format XML
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In this chapter, we describe the effect on plasmid DNA (pDNA) and oligonucleotide (ODN) transfer, of an histidine-rich peptide (H5WYG), histidylated oligolysine (HoK), and histidylated polylysine (HpK) designed on the basis of the membrane destabilization capacity of poly-L-histidine at a pH close to that of the endosomes. We report that H5WYG, which permeabilizes the cell membrane at pH 6.4, favors the transfection mediated by lactosylated polylysine/pDNA complexes and, by lowering the pH of extracellular medium, allows the loading of the cytosol and the cell nucleus with ODN. We show that HoK forms small cationic spherical particles of 35 nm with ODN and HpK rod or toroid cationic particles of 100 nm with pDNA. PEGylation stabilizes these particles at physiological salt concentration. We also show that (i) HoK/ODN complexes yield a more than 20-fold increase of the biological activity of antisense ODN towards the inhibition of transient as well as constitutive gene expression and (ii) HpK/pDNA complexes yield a transfection efficiency of 3–4.5 order of magnitude higher than do polylysine/pDNA complexes. We also provide evidence that the effect of these polyhistidylated molecules is mediated by imidazole protonation in endosomes. Overall our data show that polyhistidylated molecules constitute interesting devices for an efficient cytosolic delivery of nucleic acids, and that ionic complexes between histidylated polylysine and a pDNA are attractive for developing a nonviral gene delivery system.</div></front></TEI><istex><corpusName>springer-journals</corpusName><author><json:item><name>Patrick Midoux</name><affiliations><json:string>Centre de Biophysique Moléculaire, UPR 4301 CNRS, rue Charles Sadron, F-45071, Orléans Cedex 02, France</json:string></affiliations></json:item><json:item><name>Eric LeCam</name><affiliations><json:string>Laboratoire de Microscopie Moléculaire et Cellulaire, UMR 8532 CNRS, Institut Gustave Roussy, rue Camille Desmoulins, F-94805, Villejuif cedex, France</json:string></affiliations></json:item><json:item><name>Dominique Coulaud</name><affiliations><json:string>Laboratoire de Microscopie Moléculaire et Cellulaire, UMR 8532 CNRS, Institut Gustave Roussy, rue Camille Desmoulins, F-94805, Villejuif cedex, France</json:string></affiliations></json:item><json:item><name>Etienne Delain</name><affiliations><json:string>Laboratoire de Microscopie Moléculaire et Cellulaire, UMR 8532 CNRS, Institut Gustave Roussy, rue Camille Desmoulins, F-94805, Villejuif cedex, France</json:string></affiliations></json:item><json:item><name>Chantal Pichon</name><affiliations><json:string>Centre de Biophysique Moléculaire, UPR 4301 CNRS, rue Charles Sadron, F-45071, Orléans Cedex 02, France</json:string></affiliations></json:item></author><articleId><json:string>457015</json:string><json:string>Art4</json:string></articleId><arkIstex>ark:/67375/VQC-MDP4888L-S</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>OriginalPaper</json:string></originalGenre><abstract>Abstract: Nucleic acid transfer in mammalian cells is drastically improved with devices which increase their delivery in the cytosol upon endocytosis. 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We also show that (i) HoK/ODN complexes yield a more than 20-fold increase of the biological activity of antisense ODN towards the inhibition of transient as well as constitutive gene expression and (ii) HpK/pDNA complexes yield a transfection efficiency of 3–4.5 order of magnitude higher than do polylysine/pDNA complexes. We also provide evidence that the effect of these polyhistidylated molecules is mediated by imidazole protonation in endosomes. 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In this chapter, we describe the effect on plasmid DNA (pDNA) and oligonucleotide (ODN) transfer, of an histidine-rich peptide (H5WYG), histidylated oligolysine (HoK), and histidylated polylysine (HpK) designed on the basis of the membrane destabilization capacity of poly-L-histidine at a pH close to that of the endosomes. We report that H5WYG, which permeabilizes the cell membrane at pH 6.4, favors the transfection mediated by lactosylated polylysine/pDNA complexes and, by lowering the pH of extracellular medium, allows the loading of the cytosol and the cell nucleus with ODN. We show that HoK forms small cationic spherical particles of 35 nm with ODN and HpK rod or toroid cationic particles of 100 nm with pDNA. PEGylation stabilizes these particles at physiological salt concentration. We also show that (i) HoK/ODN complexes yield a more than 20-fold increase of the biological activity of antisense ODN towards the inhibition of transient as well as constitutive gene expression and (ii) HpK/pDNA complexes yield a transfection efficiency of 3–4.5 order of magnitude higher than do polylysine/pDNA complexes. We also provide evidence that the effect of these polyhistidylated molecules is mediated by imidazole protonation in endosomes. Overall our data show that polyhistidylated molecules constitute interesting devices for an efficient cytosolic delivery of nucleic acids, and that ionic complexes between histidylated polylysine and a pDNA are attractive for developing a nonviral gene delivery system.</p></abstract><textClass><keywords scheme="Journal Subject"><list><head>Biomedicine</head><item><term>Human Genetics</term></item><item><term>Biochemistry, general</term></item><item><term>Plant Sciences</term></item><item><term>Animal Anatomy / Morphology / Histology</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="2002-11-01">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/VQC-MDP4888L-S/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="corpus springer-journals not found" wicri:toSee="no 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Language="En">Histidine Containing Peptides and Polypeptides as Nucleic Acid Vectors</ArticleTitle><ArticleFirstPage>27</ArticleFirstPage><ArticleLastPage>47</ArticleLastPage><ArticleHistory><RegistrationDate><Year>2004</Year><Month>10</Month><Day>16</Day></RegistrationDate></ArticleHistory><ArticleCopyright><CopyrightHolderName>Plenum Publishing Corporation</CopyrightHolderName><CopyrightYear>2002</CopyrightYear></ArticleCopyright><ArticleGrants Type="Regular"><MetadataGrant Grant="OpenAccess"></MetadataGrant><AbstractGrant Grant="OpenAccess"></AbstractGrant><BodyPDFGrant Grant="Restricted"></BodyPDFGrant><BodyHTMLGrant Grant="Restricted"></BodyHTMLGrant><BibliographyGrant Grant="Restricted"></BibliographyGrant><ESMGrant Grant="Restricted"></ESMGrant></ArticleGrants><ArticleContext><JournalID>11188</JournalID><VolumeIDStart>27</VolumeIDStart><VolumeIDEnd>27</VolumeIDEnd><IssueIDStart>1</IssueIDStart><IssueIDEnd>6</IssueIDEnd></ArticleContext></ArticleInfo><ArticleHeader><AuthorGroup><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Patrick</GivenName><FamilyName>Midoux</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff2"><AuthorName DisplayOrder="Western"><GivenName>Eric</GivenName><FamilyName>LeCam</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff2"><AuthorName DisplayOrder="Western"><GivenName>Dominique</GivenName><FamilyName>Coulaud</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff2"><AuthorName DisplayOrder="Western"><GivenName>Etienne</GivenName><FamilyName>Delain</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Chantal</GivenName><FamilyName>Pichon</FamilyName></AuthorName></Author><Affiliation ID="Aff1"><OrgName>Centre de Biophysique Moléculaire</OrgName><OrgAddress><Street>UPR 4301 CNRS, rue Charles Sadron</Street><Postcode>F-45071</Postcode><City>Orléans Cedex 02</City><Country>France</Country></OrgAddress></Affiliation><Affiliation ID="Aff2"><OrgName>Laboratoire de Microscopie Moléculaire et Cellulaire</OrgName><OrgAddress><Street>UMR 8532 CNRS, Institut Gustave Roussy, rue Camille Desmoulins</Street><Postcode>F-94805</Postcode><City>Villejuif cedex</City><Country>France</Country></OrgAddress></Affiliation></AuthorGroup><Abstract ID="Abs1" Language="En"><Heading>Abstract</Heading><Para>Nucleic acid transfer in mammalian cells is drastically improved with devices which increase their delivery in the cytosol upon endocytosis. In this chapter, we describe the effect on plasmid DNA (pDNA) and oligonucleotide (ODN) transfer, of an histidine-rich peptide (H5WYG), histidylated oligolysine (HoK), and histidylated polylysine (HpK) designed on the basis of the membrane destabilization capacity of poly-L-histidine at a pH close to that of the endosomes. We report that H5WYG, which permeabilizes the cell membrane at pH 6.4, favors the transfection mediated by lactosylated polylysine/pDNA complexes and, by lowering the pH of extracellular medium, allows the loading of the cytosol and the cell nucleus with ODN. We show that HoK forms small cationic spherical particles of 35 nm with ODN and HpK rod or toroid cationic particles of 100 nm with pDNA. PEGylation stabilizes these particles at physiological salt concentration. We also show that (i) HoK/ODN complexes yield a more than 20-fold increase of the biological activity of antisense ODN towards the inhibition of transient as well as constitutive gene expression and (ii) HpK/pDNA complexes yield a transfection efficiency of 3–4.5 order of magnitude higher than do polylysine/pDNA complexes. We also provide evidence that the effect of these polyhistidylated molecules is mediated by imidazole protonation in endosomes. Overall our data show that polyhistidylated molecules constitute interesting devices for an efficient cytosolic delivery of nucleic acids, and that ionic complexes between histidylated polylysine and a pDNA are attractive for developing a nonviral gene delivery system.</Para></Abstract></ArticleHeader><NoBody></NoBody></Article></Issue></Volume></Journal></Publisher></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Histidine Containing Peptides and Polypeptides as Nucleic Acid Vectors</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Histidine Containing Peptides and Polypeptides as Nucleic Acid Vectors</title></titleInfo><name type="personal"><namePart type="given">Patrick</namePart><namePart type="family">Midoux</namePart><affiliation>Centre de Biophysique Moléculaire, UPR 4301 CNRS, rue Charles Sadron, F-45071, Orléans Cedex 02, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Eric</namePart><namePart type="family">LeCam</namePart><affiliation>Laboratoire de Microscopie Moléculaire et Cellulaire, UMR 8532 CNRS, Institut Gustave Roussy, rue Camille Desmoulins, F-94805, Villejuif cedex, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Dominique</namePart><namePart type="family">Coulaud</namePart><affiliation>Laboratoire de Microscopie Moléculaire et Cellulaire, UMR 8532 CNRS, Institut Gustave Roussy, rue Camille Desmoulins, F-94805, Villejuif cedex, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Etienne</namePart><namePart type="family">Delain</namePart><affiliation>Laboratoire de Microscopie Moléculaire et Cellulaire, UMR 8532 CNRS, Institut Gustave Roussy, rue Camille Desmoulins, F-94805, Villejuif cedex, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Chantal</namePart><namePart type="family">Pichon</namePart><affiliation>Centre de Biophysique Moléculaire, UPR 4301 CNRS, rue Charles Sadron, F-45071, Orléans Cedex 02, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="OriginalPaper" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>Kluwer Academic Publishers-Plenum Publishers</publisher><place><placeTerm type="text">New York</placeTerm></place><dateIssued encoding="w3cdtf">2002-11-01</dateIssued><copyrightDate encoding="w3cdtf">2002</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><abstract lang="en">Abstract: Nucleic acid transfer in mammalian cells is drastically improved with devices which increase their delivery in the cytosol upon endocytosis. In this chapter, we describe the effect on plasmid DNA (pDNA) and oligonucleotide (ODN) transfer, of an histidine-rich peptide (H5WYG), histidylated oligolysine (HoK), and histidylated polylysine (HpK) designed on the basis of the membrane destabilization capacity of poly-L-histidine at a pH close to that of the endosomes. We report that H5WYG, which permeabilizes the cell membrane at pH 6.4, favors the transfection mediated by lactosylated polylysine/pDNA complexes and, by lowering the pH of extracellular medium, allows the loading of the cytosol and the cell nucleus with ODN. We show that HoK forms small cationic spherical particles of 35 nm with ODN and HpK rod or toroid cationic particles of 100 nm with pDNA. PEGylation stabilizes these particles at physiological salt concentration. We also show that (i) HoK/ODN complexes yield a more than 20-fold increase of the biological activity of antisense ODN towards the inhibition of transient as well as constitutive gene expression and (ii) HpK/pDNA complexes yield a transfection efficiency of 3–4.5 order of magnitude higher than do polylysine/pDNA complexes. We also provide evidence that the effect of these polyhistidylated molecules is mediated by imidazole protonation in endosomes. Overall our data show that polyhistidylated molecules constitute interesting devices for an efficient cytosolic delivery of nucleic acids, and that ionic complexes between histidylated polylysine and a pDNA are attractive for developing a nonviral gene delivery system.</abstract><relatedItem type="host"><titleInfo><title>Somatic Cell and Molecular Genetics</title></titleInfo><titleInfo type="abbreviated"><title>Somat Cell Mol Genet</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>Springer</publisher><dateIssued encoding="w3cdtf">2002-11-01</dateIssued><copyrightDate encoding="w3cdtf">2002</copyrightDate></originInfo><subject><genre>Biomedicine</genre><topic>Human Genetics</topic><topic>Biochemistry, general</topic><topic>Plant Sciences</topic><topic>Animal Anatomy / Morphology / Histology</topic></subject><identifier type="ISSN">0740-7750</identifier><identifier type="eISSN">1572-9931</identifier><identifier type="JournalID">11188</identifier><identifier type="IssueArticleCount">10</identifier><identifier type="VolumeIssueCount">6</identifier><part><date>2002</date><detail type="volume"><number>27</number><caption>vol.</caption></detail><detail type="issue"><number>1-6</number><caption>no.</caption></detail><extent unit="pages"><start>27</start><end>47</end></extent></part><recordInfo><recordOrigin>Plenum Publishing Corporation, 2002</recordOrigin></recordInfo></relatedItem><identifier type="istex">09F94AE257E55C800B44108232926C0C6411CA96</identifier><identifier type="ark">ark:/67375/VQC-MDP4888L-S</identifier><identifier type="DOI">10.1023/A:1022931923153</identifier><identifier type="ArticleID">457015</identifier><identifier type="ArticleID">Art4</identifier><accessCondition type="use and reproduction" contentType="copyright">Plenum Publishing Corporation, 2002</accessCondition><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-3XSW68JL-F">springer</recordContentSource><recordOrigin>Plenum Publishing Corporation, 2002</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/VQC-MDP4888L-S/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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