Back to Search
Start Over
The strand transfer oligonucleotide inhibitors of HIV-integrase.
- Source :
-
Journal of Enzyme Inhibition & Medicinal Chemistry . Feb2009, Vol. 24 Issue 1, p241-246. 6p. 1 Diagram, 1 Chart, 2 Graphs. - Publication Year :
- 2009
-
Abstract
- Retroviral integrase participates in two catalytic reactions, which require interactions with the two ends of the viral DNA in the 3'processing reaction, and with a targeted host DNA in the strand transfer reaction. The 3'-hydroxyl group of 2'-deoxyadenosine resulting from the specific removing of GT dinucleotide from the viral DNA in the processing reaction provides the attachment site for the host DNA in a transesterification reaction. We synthesized oligonucleotides (ONs) of various lengths that mimic the processed HIV-1 U5 terminus of the proviral long terminal repeat (LTR) and are ended by 2'-deoxyadenosine containing a 3'-O-phosphonomethyl group. The duplex stability of phosphonomethyl ONs was increased by covalent linkage of the modified strand with its complementary strand by a triethylene glycol loop (TEG). Modified ONs containing up to 10 bases inhibited in vitro the strand transfer reaction catalyzed by HIV-1 integrase at nanomolar concentrations. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 14756366
- Volume :
- 24
- Issue :
- 1
- Database :
- Academic Search Index
- Journal :
- Journal of Enzyme Inhibition & Medicinal Chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 131854925
- Full Text :
- https://doi.org/10.1080/14756360802051578