BIOL 116 |
| In retroviruses such as HIV, disrupting certain RNA-protein or RNA-RNA interactions responsible for viral replication with small molecules may lead to new therapeutics. Our efforts have been focused on the HIV-1 Dimerization Initiation Site (DIS), a potential RNA target that is involved with reverse transcription and viral encapsidation. Recent x-ray crystal structures reveal strong similarity between the DIS and the prokaryotic A-site, an RNA construct where most aminoglycoside antibiotics bind. Due to structural homology, we theorize that the established fluorescence assay of monitoring small molecule binding to the A-site can also be achieved with the DIS. We now report the design and results of a fluorescence-based assay that quantifies binding of aminoglycosides to the HIV-1 DIS. |
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Chemistry and Metabolism
4:30 PM-6:30 PM, Tuesday, 12 September 2006 Moscone Center -- Hall D, Poster
Division of Biological Chemistry |