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Esposito, F./ A. Corona/ L. Zinzula/ T. Kharlamova/ E. Tramontano 2012: New anthraquinone derivatives as inhibitors of the HIV-1 reverse transcriptase-associated ribonuclease H function. - Chemotherapy 58(4): 299-307. [RLL List # 231 / Rec.# 34604]
Keywords: Anthraquinone derivatives/ HIV-1/ Reverse transcriptase/ Ribonuclease H/ RNase H/ alizarin/ anthraquinone derivative/ ribonuclease H/ RNA directed DNA polymerase/ article/ drug determination/ drug inhibition/ drug potency/ enzyme activity/ enzyme inhibition/ Human immunodeficiency virus 1/ IC 50/ nonhuman/ priority journal/ protein function/ virus inhibition
Abstract: Background: The degradative activity of the human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT), termed ribonuclease H (RNase H), which hydrolyzes the RNA component of the heteroduplex RNA:DNA replication intermediate, is an excellent target for drug discovery. Anthraquinones (AQs) and their derivatives, which are common secondary metabolites occurring in bacteria, fungi, lichens and a large number of families in higher plants, have been reported to have several biological activities including that of inhibiting HIV-1 RT activities in biochemical assays. Methods: We have assayed new AQ derivatives on HIV-1 RNase H activities in biochemical assays. Results: Six series of new AQ derivatives with various substituents at positions 1, 2, 3 and 4 of the AQ ring were tested, and new analogs able to inhibit HIV-1 RT-associated RNase H activity in the low micromolar range were found. Conclusions: Our results demonstrate that AQ derivatives are promising anti-RNase H inhibitors. © 2012 S. Karger AG, Basel.
URL: http://dx.doi.org/10.1159/000343101
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