Template. Phosphorothioate oligonucleotides duplexes as inhibitors of HIV-1 reverse transcriptase.
Identifieur interne : 002951 ( PubMed/Corpus ); précédent : 002950; suivant : 002952Template. Phosphorothioate oligonucleotides duplexes as inhibitors of HIV-1 reverse transcriptase.
Auteurs : G. Maury ; A. El Alaoui ; F. Morvan ; B. Müller ; J L Imbach ; R S GoodySource :
- Biochemical and biophysical research communications [ 0006-291X ] ; 1992.
English descriptors
- KwdEn :
- Antiviral Agents (pharmacology), Base Sequence, HIV Reverse Transcriptase, Kinetics, Molecular Sequence Data, Nucleic Acid Denaturation, Oligodeoxyribonucleotides (pharmacology), Polydeoxyribonucleotides (metabolism), Recombinant Proteins (antagonists & inhibitors), Reverse Transcriptase Inhibitors, Templates, Genetic, Thermodynamics, Thionucleotides.
- MESH :
- chemical , antagonists & inhibitors : Recombinant Proteins.
- chemical , metabolism : Polydeoxyribonucleotides.
- chemical , pharmacology : Antiviral Agents, Oligodeoxyribonucleotides.
- Base Sequence, HIV Reverse Transcriptase, Kinetics, Molecular Sequence Data, Nucleic Acid Denaturation, Reverse Transcriptase Inhibitors, Templates, Genetic, Thermodynamics, Thionucleotides.
Abstract
We have investigated the interaction between a number of 14 mers phosphorothioate oligonucleotides and HIV-1 reverse transcriptase. Two methods were used to measure the affinity of the analogs for the enzyme. In the first, the oligonucleotide or its duplex with Poly(rl) were used as inhibitors of the enzyme using Poly(rA).(dT)14 as template primer. In the second, the oligonucleotides or their duplexes were used to displace a fluorescent template primer complex of known affinity from its binding site on reverse transcriptase. The two methods gave the same relative order of affinity. Phosphorothioate oligodeoxyribonucleotides had a much higher affinity than oligo(dC)14 and it was increased on hybridization. Quantitatively similar results were obtained for S(dC)14 or its analog with bases in the alpha-configuration. Of the analogs tested, only S(dC)14 showed priming activity.
DOI: 10.1016/s0006-291x(05)81540-2
PubMed: 1380799
Links to Exploration step
pubmed:1380799Le document en format XML
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<author><name sortKey="Maury, G" sort="Maury, G" uniqKey="Maury G" first="G" last="Maury">G. Maury</name>
<affiliation><nlm:affiliation>Université de Montpellier II, URA 488 du CNRS, Département de Chimie Organique Fine, France.</nlm:affiliation>
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<author><name sortKey="El Alaoui, A" sort="El Alaoui, A" uniqKey="El Alaoui A" first="A" last="El Alaoui">A. El Alaoui</name>
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<author><name sortKey="Morvan, F" sort="Morvan, F" uniqKey="Morvan F" first="F" last="Morvan">F. Morvan</name>
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<author><name sortKey="Muller, B" sort="Muller, B" uniqKey="Muller B" first="B" last="Müller">B. Müller</name>
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<author><name sortKey="Imbach, J L" sort="Imbach, J L" uniqKey="Imbach J" first="J L" last="Imbach">J L Imbach</name>
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<author><name sortKey="Goody, R S" sort="Goody, R S" uniqKey="Goody R" first="R S" last="Goody">R S Goody</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Template. Phosphorothioate oligonucleotides duplexes as inhibitors of HIV-1 reverse transcriptase.</title>
<author><name sortKey="Maury, G" sort="Maury, G" uniqKey="Maury G" first="G" last="Maury">G. Maury</name>
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<author><name sortKey="Imbach, J L" sort="Imbach, J L" uniqKey="Imbach J" first="J L" last="Imbach">J L Imbach</name>
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<series><title level="j">Biochemical and biophysical research communications</title>
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<term>HIV Reverse Transcriptase</term>
<term>Kinetics</term>
<term>Molecular Sequence Data</term>
<term>Nucleic Acid Denaturation</term>
<term>Oligodeoxyribonucleotides (pharmacology)</term>
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<term>Templates, Genetic</term>
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<term>Oligodeoxyribonucleotides</term>
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<keywords scheme="MESH" xml:lang="en"><term>Base Sequence</term>
<term>HIV Reverse Transcriptase</term>
<term>Kinetics</term>
<term>Molecular Sequence Data</term>
<term>Nucleic Acid Denaturation</term>
<term>Reverse Transcriptase Inhibitors</term>
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<front><div type="abstract" xml:lang="en">We have investigated the interaction between a number of 14 mers phosphorothioate oligonucleotides and HIV-1 reverse transcriptase. Two methods were used to measure the affinity of the analogs for the enzyme. In the first, the oligonucleotide or its duplex with Poly(rl) were used as inhibitors of the enzyme using Poly(rA).(dT)14 as template primer. In the second, the oligonucleotides or their duplexes were used to displace a fluorescent template primer complex of known affinity from its binding site on reverse transcriptase. The two methods gave the same relative order of affinity. Phosphorothioate oligodeoxyribonucleotides had a much higher affinity than oligo(dC)14 and it was increased on hybridization. Quantitatively similar results were obtained for S(dC)14 or its analog with bases in the alpha-configuration. Of the analogs tested, only S(dC)14 showed priming activity.</div>
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<Abstract><AbstractText>We have investigated the interaction between a number of 14 mers phosphorothioate oligonucleotides and HIV-1 reverse transcriptase. Two methods were used to measure the affinity of the analogs for the enzyme. In the first, the oligonucleotide or its duplex with Poly(rl) were used as inhibitors of the enzyme using Poly(rA).(dT)14 as template primer. In the second, the oligonucleotides or their duplexes were used to displace a fluorescent template primer complex of known affinity from its binding site on reverse transcriptase. The two methods gave the same relative order of affinity. Phosphorothioate oligodeoxyribonucleotides had a much higher affinity than oligo(dC)14 and it was increased on hybridization. Quantitatively similar results were obtained for S(dC)14 or its analog with bases in the alpha-configuration. Of the analogs tested, only S(dC)14 showed priming activity.</AbstractText>
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