ArticleBioorganic & medicinal chemistry letters2015
Molecular docking and antiviral activity of N-substituted benzyl/phenyl-2-(3,4-dimethyl-5,5-dioxidopyrazolo[4,3-c][1,2]benzothiazin-2(4H)-yl)acetamides.
Article in Bioorganic & medicinal chemistry letters, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed, 35 citations in OpenAlex.
- 1,2-Benzothiazine Derivatives as Anti-HIV and Anti-HCV Agents: Structure-Activity Relationships and Research Perspectives.International journal of molecular sciences · 2026Review
- An insight into the synthetic routes for N-arylation of morpholine using metal-catalyzed and metal-free methods.Molecular diversity · 2026Review
- Anti-Inflammatory Activity of 1,2-Benzothiazine 1,1-Dioxide Derivatives.Pharmaceuticals (Basel, Switzerland) · 2025Review
- Recent synthetic strategies for N-arylation of pyrrolidines: a potential template for biologically active molecules.Molecular diversity · 2025Review
- Article
- Identification of Cyclic Sulfonamides with anPharmaceuticals (Basel, Switzerland) · 2022Article
Corrections and comments
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Authors and funding
10 authors at 5 institutions in 2 countries.
Funding
Abstract
Two series of fifteen N-substituted benzyl/phenyl-2-(3,4-dimethyl-5,5-dioxidopyrazolo[4,3-c][1,2]benzothiazin-2(4H)-yl)acetamides were screened for anti-HIV-1 activity and cytotoxicity. The compounds 6a, 6d, 6e, 6g and 6i from the series 6a-i of benzylamides and 7a, 7b, 7c, 7d and 7e from the series 7a-f of anilides were identified as effective anti-HIV-1 agents with EC50 values <20μM. Among these compounds that displayed anti-HIV-1 activity, 6a, 6e, 6g and 6i showed no toxicity in human PBM, CEM and Vero cells, with the exception of 6a which displayed toxicity in Vero cells. Molecular docking of these compounds provided insight into the molecular mechanism and it was found that 6e, 6g and 6i bound deeply in the NNRTI binding pocket of the HIV-1 reverse transcriptase, using RT-bound nevirapine X-ray data and molecular docking for validation, showing the potential of these new structures as inhibitors of this viral enzyme.
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