Author: Ross D. Overacker; Somdev Banerjee; George F. Neuhaus; Selena Milicevic Sephton; Alexander Herrmann; James A. Strother; Ruth Brack-Werner; Paul R. Blakemore; Sandra Loesgen
Title: Biological Evaluation of Molecules of the azaBINOL Class as Antiviral Agents: Specific Inhibition of HIV-1 RNase H Activity by 7-Isopropoxy-8-(naphth-1-yl)quinoline Document date: 2019_1_23
ID: m2zw8eq4_33
Snippet: identified RNase H inhibition, direct HIV-1 RT binding, and the known hydrophobic binding 309 surfaces associated with allosteric inhibiton, 58 we believe that B#24 is a novel allosteric inhibitor 310 of HIV-1 RT-RNase H activity. While biaryl compounds of natural origin have long been known 311 to exhibit significant biological activity, 14, 61 this study suggests that further investigations of the 312 bioactivity of artificial biaryls, designed.....
Document: identified RNase H inhibition, direct HIV-1 RT binding, and the known hydrophobic binding 309 surfaces associated with allosteric inhibiton, 58 we believe that B#24 is a novel allosteric inhibitor 310 of HIV-1 RT-RNase H activity. While biaryl compounds of natural origin have long been known 311 to exhibit significant biological activity, 14, 61 this study suggests that further investigations of the 312 bioactivity of artificial biaryls, designed purely with synthetic utility in mind, are warranted. The copyright holder for this preprint (which was not peer-reviewed) is the author/funder. . https://doi.org/10.1101/525105 doi: bioRxiv preprint followed by TLC analysis using silica gel 60 plates (2-25 µm) with fluorescent indicator (254 329 nm) and visualized by UV or phosphomolybdic acid (PMA). 330
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