(s4dU)35: a novel, highly potent oligonucleotide inhibitor of the human immunodeficiency virus type 1 reverse transcriptase
Identifieur interne : 003F09 ( Main/Curation ); précédent : 003F08; suivant : 003F10(s4dU)35: a novel, highly potent oligonucleotide inhibitor of the human immunodeficiency virus type 1 reverse transcriptase
Auteurs : Szilvia Tökés [Hongrie] ; Janos Aradi [Hongrie]Source :
- FEBS Letters [ 0014-5793 ] ; 1996.
English descriptors
- Teeft :
- Agents chemother, Alkaline phosphatase, Chain length, Chemical modification, Competitive inhibitors, Data points, Dixon plot, Free enzyme, Hplc analysis, Human immunodeficiency virus type, Inhibitor, Inhibitory, Inhibitory activity, Large number, Minute amount, Nucleic acids, Oligonucleotides, Potent inhibitors, Protein synthesis, Transcriptase, Unmodified base, Variable substrate.
Abstract
Abstract: Oligodeoxycytidylates were converted to s4dUMP-containing oligomers by treatment with liquid H2S. The inhibitory potency of the modified oligonucleotides on human immunodeficiency virus type 1 reverse transcriptase depended on the chain length and on the percentage of modification. The most potent reverse transcriptase inhibitor was (s4dU)35. The inhibitory pattern was competitive, when either poly(A)·(dT)16 or poly(C)·(dG)16 was used as template-primer (variable substrate), suggesting that the free enzyme interacts with (s4dU)35. The Ki values were 3.0 and 2.2 nM in the presence of poly(A)·(dT)16 and poly(C)·(dG)16, respectively.
Url:
DOI: 10.1016/0014-5793(96)01032-0
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<front><div type="abstract" xml:lang="en">Abstract: Oligodeoxycytidylates were converted to s4dUMP-containing oligomers by treatment with liquid H2S. The inhibitory potency of the modified oligonucleotides on human immunodeficiency virus type 1 reverse transcriptase depended on the chain length and on the percentage of modification. The most potent reverse transcriptase inhibitor was (s4dU)35. The inhibitory pattern was competitive, when either poly(A)·(dT)16 or poly(C)·(dG)16 was used as template-primer (variable substrate), suggesting that the free enzyme interacts with (s4dU)35. The Ki values were 3.0 and 2.2 nM in the presence of poly(A)·(dT)16 and poly(C)·(dG)16, respectively.</div>
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