Biochem Biophys Res Commun. 1992 Aug 14;186(3):1249-56. Unique
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.
Antiviral Agents/*PHARMACOLOGY Base Sequence Kinetics Molecular
Sequence Data Nucleic Acid Denaturation
Polydeoxyribonucleotides/METABOLISM Recombinant Proteins/ANTAGONISTS &
INHIB RNA-Directed DNA Polymerase/*ANTAGONISTS & INHIB Support,
Non-U.S. Gov't Templates Thermodynamics Thionucleotides JOURNAL