CARB 109 |
| The Reverse Transcriptase (RT) of the Human Immunodeficiency Virus (HIV) has both polymerase and RNase H activity. Current antiviral regimens rely heavily on agents that target the polymerase activity of HIV RT. Due to the high rate of mutation of HIV RT, resistant strains emerge against current therapies. Therefore, there is a great need for the development of new antiretroviral agents. Although RT can accommodate nucleic acids in both of its active sites, our lab has shown that small RNA hairpins can selectively inhibit the RNase H activity associated with HIV-1 RT. We now show how second generation compounds are being developed for therapeutic applications and can be tuned for potency and specificity by chemically modifying the native RNA hairpin. In addition, the mode of action of the hairpins is investigated in detail. The merits of targeting the RNase H activity and the potential for using this in combination with current strategies are also addressed. |
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Carbohydrate Chemistry and Biochemistry
8:30 AM-11:50 AM, Thursday, August 23, 2007 BCEC -- 162B, Oral
Division of Carbohydrate Chemistry |