In vitro and in silico investigation of interferonogenic analogues of nucleic acids, artificially programmed to block the initial stages of HIV infection of cells
Identifieur interne : 001261 ( Istex/Corpus ); précédent : 001260; suivant : 001262In vitro and in silico investigation of interferonogenic analogues of nucleic acids, artificially programmed to block the initial stages of HIV infection of cells
Auteurs : A. V. Serbin ; A. V. Veselovskii ; V. B. TsvetkovSource :
- Applied Biochemistry and Microbiology [ 0003-6838 ] ; 2012-12-01.
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Abstract
Abstract: Approaches to the molecular design of antiviral agents based on the principals of adequacy and mimicry to biopolymers have been discussed. The approaches permit for the reproduction of pharmaceutically valuable properties of the polymeric basis (core) and to create novel nongenetic “programs” of bioactivity of macromolecules by means of grafting specific side group combinations to this core. In vivo experiments have shown that the immunostimulating (in particular, interferon-inducing) antiviral potency of nucleic acids (NAs) is a characteristic of carboxylic acid analogues with an NA-type order of furan and anionic component alteration in the polymer chain. Controlled grafting of virus-targeted side groups of the polymeric basis leads to the direct blockage of viral infection in vitro as an additional antiviral effect. In this work, the inhibition of the early penetration stages of human immunodeficiency virus type 1 (HIV-1) in cells has been studied. Modelling of the macromolecule interaction with the most probable target (the virus-cell fusion mediator (an α-helical complex of the N- heptad repeat regions of three HIV-1 envelope glycoprotein gp41 transmembrane molecules) was performed. Computational docking of the experiment in silico resulted in the clarification of the putative mechanisms and parameters for the programming of site-tropic, axial, and belting blockages of the target via the application of an alicyclic-type side group. The discovered opportunities of multipoint axial cobelting blockage of a target opens up new prospects for the prevention/therapy of AIDS, as well as for other viral infections that use similar systems of envelope fusion peptides (of the first and third types) for penetration into cells.
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DOI: 10.1134/S0003683812090049
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ISTEX:C1F438D354D3B3D8CAD1F9431E3E569E6FBF3D5ELe document en format XML
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V." last="Serbin">A. V. Serbin</name><affiliation><mods:affiliation>Biomodulators and Drugs Research Center, Health Research & Development Foundation, 117042, Moscow, Russia</mods:affiliation></affiliation><affiliation><mods:affiliation>Topchiev Institute of Petrochemical Synthesis, Russian Academy of Sciences, 119991, Moscow, Russia</mods:affiliation></affiliation><affiliation><mods:affiliation>E-mail: heal@aha.ru</mods:affiliation></affiliation></author><author><name sortKey="Veselovskii, A V" sort="Veselovskii, A V" uniqKey="Veselovskii A" first="A. V." last="Veselovskii">A. V. Veselovskii</name><affiliation><mods:affiliation>Orekhovich Institute of Biomedical Chemistry, Russian Academy of Medical Sciences, 119121, Moscow, Russia</mods:affiliation></affiliation></author><author><name sortKey="Tsvetkov, V B" sort="Tsvetkov, V B" uniqKey="Tsvetkov V" first="V. B." last="Tsvetkov">V. B. 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The approaches permit for the reproduction of pharmaceutically valuable properties of the polymeric basis (core) and to create novel nongenetic “programs” of bioactivity of macromolecules by means of grafting specific side group combinations to this core. In vivo experiments have shown that the immunostimulating (in particular, interferon-inducing) antiviral potency of nucleic acids (NAs) is a characteristic of carboxylic acid analogues with an NA-type order of furan and anionic component alteration in the polymer chain. Controlled grafting of virus-targeted side groups of the polymeric basis leads to the direct blockage of viral infection in vitro as an additional antiviral effect. In this work, the inhibition of the early penetration stages of human immunodeficiency virus type 1 (HIV-1) in cells has been studied. Modelling of the macromolecule interaction with the most probable target (the virus-cell fusion mediator (an α-helical complex of the N- heptad repeat regions of three HIV-1 envelope glycoprotein gp41 transmembrane molecules) was performed. Computational docking of the experiment in silico resulted in the clarification of the putative mechanisms and parameters for the programming of site-tropic, axial, and belting blockages of the target via the application of an alicyclic-type side group. The discovered opportunities of multipoint axial cobelting blockage of a target opens up new prospects for the prevention/therapy of AIDS, as well as for other viral infections that use similar systems of envelope fusion peptides (of the first and third types) for penetration into cells.</div></front></TEI><istex><corpusName>springer-journals</corpusName><author><json:item><name>A. V. 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Modelling of the macromolecule interaction with the most probable target (the virus-cell fusion mediator (an α-helical complex of the N- heptad repeat regions of three HIV-1 envelope glycoprotein gp41 transmembrane molecules) was performed. Computational docking of the experiment in silico resulted in the clarification of the putative mechanisms and parameters for the programming of site-tropic, axial, and belting blockages of the target via the application of an alicyclic-type side group. 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The approaches permit for the reproduction of pharmaceutically valuable properties of the polymeric basis (core) and to create novel nongenetic “programs” of bioactivity of macromolecules by means of grafting specific side group combinations to this core. In vivo experiments have shown that the immunostimulating (in particular, interferon-inducing) antiviral potency of nucleic acids (NAs) is a characteristic of carboxylic acid analogues with an NA-type order of furan and anionic component alteration in the polymer chain. Controlled grafting of virus-targeted side groups of the polymeric basis leads to the direct blockage of viral infection in vitro as an additional antiviral effect. In this work, the inhibition of the early penetration stages of human immunodeficiency virus type 1 (HIV-1) in cells has been studied. Modelling of the macromolecule interaction with the most probable target (the virus-cell fusion mediator (an α-helical complex of the N- heptad repeat regions of three HIV-1 envelope glycoprotein gp41 transmembrane molecules) was performed. Computational docking of the experiment in silico resulted in the clarification of the putative mechanisms and parameters for the programming of site-tropic, axial, and belting blockages of the target via the application of an alicyclic-type side group. The discovered opportunities of multipoint axial cobelting blockage of a target opens up new prospects for the prevention/therapy of AIDS, as well as for other viral infections that use similar systems of envelope fusion peptides (of the first and third types) for penetration into cells.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Keywords</head><item><term>alternating maleic acid copolymers</term></item><item><term>cage alicycles</term></item><item><term>docking</term></item><item><term>gp41</term></item><item><term>glycoprotein of the HIV envelope</term></item><item><term>modelling</term></item><item><term>virus-cell fusion inhibitors</term></item></list></keywords></textClass><textClass><keywords scheme="Journal-Subject-Collection"><list><label>Biomedical and Life Sciences</label><item><term>SC3</term></item></list></keywords></textClass><textClass><keywords scheme="Journal Subject"><list><head>Life 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silico investigation of interferonogenic analogues of nucleic acids, artificially programmed to block the initial stages of HIV infection of cells</ArticleTitle><ArticleFirstPage>723</ArticleFirstPage><ArticleLastPage>739</ArticleLastPage><ArticleHistory><RegistrationDate><Year>2012</Year><Month>11</Month><Day>4</Day></RegistrationDate><Received><Year>2011</Year><Month>8</Month><Day>4</Day></Received><OnlineDate><Year>2012</Year><Month>11</Month><Day>6</Day></OnlineDate></ArticleHistory><ArticleCopyright><CopyrightHolderName>Pleiades Publishing, Ltd.</CopyrightHolderName><CopyrightYear>2012</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></ArticleInfo><ArticleHeader><AuthorGroup><Author AffiliationIDS="Aff1 Aff2" CorrespondingAffiliationID="Aff1"><AuthorName DisplayOrder="Western"><GivenName>A.</GivenName><GivenName>V.</GivenName><FamilyName>Serbin</FamilyName></AuthorName><Contact><Email>heal@aha.ru</Email></Contact></Author><Author AffiliationIDS="Aff3"><AuthorName DisplayOrder="Western"><GivenName>A.</GivenName><GivenName>V.</GivenName><FamilyName>Veselovskii</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1 Aff3"><AuthorName DisplayOrder="Western"><GivenName>V.</GivenName><GivenName>B.</GivenName><FamilyName>Tsvetkov</FamilyName></AuthorName></Author><Affiliation ID="Aff1"><OrgDivision>Biomodulators and Drugs Research Center</OrgDivision><OrgName>Health Research & Development Foundation</OrgName><OrgAddress><City>Moscow</City><Postcode>117042</Postcode><Country Code="RU">Russia</Country></OrgAddress></Affiliation><Affiliation ID="Aff2"><OrgDivision>Topchiev Institute of Petrochemical Synthesis</OrgDivision><OrgName>Russian Academy of Sciences</OrgName><OrgAddress><City>Moscow</City><Postcode>119991</Postcode><Country Code="RU">Russia</Country></OrgAddress></Affiliation><Affiliation ID="Aff3"><OrgDivision>Orekhovich Institute of Biomedical Chemistry</OrgDivision><OrgName>Russian Academy of Medical Sciences</OrgName><OrgAddress><City>Moscow</City><Postcode>119121</Postcode><Country Code="RU">Russia</Country></OrgAddress></Affiliation></AuthorGroup><Abstract ID="Abs1" Language="En"><Heading>Abstract</Heading><Para>Approaches to the molecular design of antiviral agents based on the principals of adequacy and mimicry to biopolymers have been discussed. The approaches permit for the reproduction of pharmaceutically valuable properties of the polymeric basis (core) and to create novel nongenetic “programs” of bioactivity of macromolecules by means of grafting specific side group combinations to this core. In vivo experiments have shown that the immunostimulating (in particular, interferon-inducing) antiviral potency of nucleic acids (NAs) is a characteristic of carboxylic acid analogues with an NA-type order of furan and anionic component alteration in the polymer chain. Controlled grafting of virus-targeted side groups of the polymeric basis leads to the direct blockage of viral infection in vitro as an additional antiviral effect. In this work, the inhibition of the early penetration stages of human immunodeficiency virus type 1 (HIV-1) in cells has been studied. Modelling of the macromolecule interaction with the most probable target (the virus-cell fusion mediator (an α-helical complex of the N- heptad repeat regions of three HIV-1 envelope glycoprotein gp41 transmembrane molecules) was performed. Computational docking of the experiment in silico resulted in the clarification of the putative mechanisms and parameters for the programming of site-tropic, axial, and belting blockages of the target via the application of an alicyclic-type side group. The discovered opportunities of multipoint axial cobelting blockage of a target opens up new prospects for the prevention/therapy of AIDS, as well as for other viral infections that use similar systems of envelope fusion peptides (of the first and third types) for penetration into cells.</Para></Abstract><KeywordGroup Language="En"><Heading>Keywords</Heading><Keyword>alternating maleic acid copolymers</Keyword><Keyword>cage alicycles</Keyword><Keyword>docking</Keyword><Keyword>gp41</Keyword><Keyword>glycoprotein of the HIV envelope</Keyword><Keyword>modelling</Keyword><Keyword>virus-cell fusion inhibitors</Keyword></KeywordGroup><ArticleNote Type="Misc"><SimplePara>Original Russian Text © A.V. Serbin, A.V. Veselovskii, V.B. Tsvetkov, 2012, published in Biotekhnologiya, 2012, No. 1, pp. 72–89.</SimplePara></ArticleNote></ArticleHeader><NoBody></NoBody></Article></Issue></Volume></Journal></Publisher></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>In vitro and in silico investigation of interferonogenic analogues of nucleic acids, artificially programmed to block the initial stages of HIV infection of cells</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>In vitro and in silico investigation of interferonogenic analogues of nucleic acids, artificially programmed to block the initial stages of HIV infection of cells</title></titleInfo><name type="personal" displayLabel="corresp"><namePart type="given">A.</namePart><namePart type="given">V.</namePart><namePart type="family">Serbin</namePart><affiliation>Biomodulators and Drugs Research Center, Health Research & Development Foundation, 117042, Moscow, Russia</affiliation><affiliation>Topchiev Institute of Petrochemical Synthesis, Russian Academy of Sciences, 119991, Moscow, Russia</affiliation><affiliation>E-mail: heal@aha.ru</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">A.</namePart><namePart type="given">V.</namePart><namePart type="family">Veselovskii</namePart><affiliation>Orekhovich Institute of Biomedical Chemistry, Russian Academy of Medical Sciences, 119121, Moscow, Russia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">V.</namePart><namePart type="given">B.</namePart><namePart type="family">Tsvetkov</namePart><affiliation>Biomodulators and Drugs Research Center, Health Research & Development Foundation, 117042, Moscow, Russia</affiliation><affiliation>Orekhovich Institute of Biomedical Chemistry, Russian Academy of Medical Sciences, 119121, Moscow, Russia</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>SP MAIK Nauka/Interperiodica</publisher><place><placeTerm type="text">Dordrecht</placeTerm></place><dateCreated encoding="w3cdtf">2011-08-04</dateCreated><dateIssued encoding="w3cdtf">2012-12-01</dateIssued><copyrightDate encoding="w3cdtf">2012</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><abstract lang="en">Abstract: Approaches to the molecular design of antiviral agents based on the principals of adequacy and mimicry to biopolymers have been discussed. The approaches permit for the reproduction of pharmaceutically valuable properties of the polymeric basis (core) and to create novel nongenetic “programs” of bioactivity of macromolecules by means of grafting specific side group combinations to this core. In vivo experiments have shown that the immunostimulating (in particular, interferon-inducing) antiviral potency of nucleic acids (NAs) is a characteristic of carboxylic acid analogues with an NA-type order of furan and anionic component alteration in the polymer chain. Controlled grafting of virus-targeted side groups of the polymeric basis leads to the direct blockage of viral infection in vitro as an additional antiviral effect. In this work, the inhibition of the early penetration stages of human immunodeficiency virus type 1 (HIV-1) in cells has been studied. Modelling of the macromolecule interaction with the most probable target (the virus-cell fusion mediator (an α-helical complex of the N- heptad repeat regions of three HIV-1 envelope glycoprotein gp41 transmembrane molecules) was performed. Computational docking of the experiment in silico resulted in the clarification of the putative mechanisms and parameters for the programming of site-tropic, axial, and belting blockages of the target via the application of an alicyclic-type side group. The discovered opportunities of multipoint axial cobelting blockage of a target opens up new prospects for the prevention/therapy of AIDS, as well as for other viral infections that use similar systems of envelope fusion peptides (of the first and third types) for penetration into cells.</abstract><subject lang="en"><genre>Keywords</genre><topic>alternating maleic acid copolymers</topic><topic>cage alicycles</topic><topic>docking</topic><topic>gp41</topic><topic>glycoprotein of the HIV envelope</topic><topic>modelling</topic><topic>virus-cell fusion inhibitors</topic></subject><relatedItem type="host"><titleInfo><title>Applied Biochemistry and Microbiology</title></titleInfo><titleInfo type="abbreviated"><title>Appl Biochem Microbiol</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">2012-11-06</dateIssued><copyrightDate encoding="w3cdtf">2012</copyrightDate></originInfo><subject><genre>Journal-Subject-Collection</genre><topic authority="SpringerSubjectCodes" authorityURI="Biomedical and Life Sciences">SC3</topic></subject><subject><genre>Life Sciences</genre><topic>Microbiology</topic><topic>Biochemistry, general</topic><topic>Medical Microbiology</topic></subject><identifier type="ISSN">0003-6838</identifier><identifier type="eISSN">1608-3024</identifier><identifier type="JournalID">10438</identifier><identifier type="IssueArticleCount">5</identifier><identifier type="VolumeIssueCount">9</identifier><part><date>2012</date><detail type="volume"><number>48</number><caption>vol.</caption></detail><detail type="issue"><number>9</number><caption>no.</caption></detail><extent unit="pages"><start>723</start><end>739</end></extent></part><recordInfo><recordOrigin>Pleiades Publishing, Ltd., 2012</recordOrigin></recordInfo></relatedItem><identifier type="istex">C1F438D354D3B3D8CAD1F9431E3E569E6FBF3D5E</identifier><identifier type="ark">ark:/67375/VQC-H8R1N5M4-M</identifier><identifier type="DOI">10.1134/S0003683812090049</identifier><identifier type="ArticleID">6452</identifier><identifier type="ArticleID">S0003683812090049</identifier><accessCondition type="use and reproduction" contentType="copyright">Pleiades Publishing, Ltd., 2012</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>Pleiades Publishing, Ltd., 2012</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/VQC-H8R1N5M4-M/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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