Me-Better Drug Design Based on Nevirapine and Mechanism of Molecular Interactions with Y188C Mutant HIV-1 Reverse Transcriptase.

Yan Wang, Aidong Wang, Jianhua Wang, Xiaoran Wu, Yijie Sun, Yan Wu

Abstract read

In one paragraph

Article in Molecules (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing papers in PubMed

–field-weighted citation impact

1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

Medicinal Chemistry Aspects of Thiazole and Thiazolidine Derivatives as Fundamental Building Blocks to Design New NNRTIs Against HIV-1 Reverse Transcriptase.ChemMedChem · 2026
Review

4 · The record

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PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Yan WangKey Laboratory of Drug Design, College of Chemistry and Chemical Engineering, Huangshan University, Huangshan 245061, China.

Aidong WangKey Laboratory of Drug Design, College of Chemistry and Chemical Engineering, Huangshan University, Huangshan 245061, China.

Jianhua WangKey Laboratory of Biorheological Science and Technology, Ministry of Education, Chongqing University, Chongqing 400044, China.ORCID 0000-0002-0459-7145

Xiaoran WuKey Laboratory of Drug Design, College of Chemistry and Chemical Engineering, Huangshan University, Huangshan 245061, China.

Yijie SunKey Laboratory of Drug Design, College of Chemistry and Chemical Engineering, Huangshan University, Huangshan 245061, China.

Yan WuKey Laboratory of Drug Design, College of Chemistry and Chemical Engineering, Huangshan University, Huangshan 245061, China.

Funding

Huangshan Technological Innovation Center of Xin'an Traditional Chinese Medicine hsjszx202003Key Laboratory of pharmaceutical design kypt201810Natural Science Research Program of Colleges and Universities in Anhui Province KJ2021ZD0121Natural Science Research Program of Colleges and Universities in Anhui Province KJHS2021B11Natural Science Research Program of Colleges and Universities in Anhui Province KJHS2021B12Natural Science Research Program of Huangshan University 2020xkjq018Provincial Quality Engineering Fund 2020xfxm67

6 · The paper itself

Abstract

In this paper, the Y188C mutant HIV-1 reverse transcriptase (Y188CM-RT) target protein was constructed by homology modeling, and new ligands based on nevirapine (NVP) skeleton were designed by means of fragment growth. The binding activity of new ligands to Y188CM-RT was evaluated by structural analysis, ADMET prediction, molecular docking, energy calculation and molecular dynamics. Results show that 10 new ligands had good absorbability, and their binding energies to Y188CM-RT were significantly higher than those of wild-type HIV-1 reverse transcriptase(wt). The binding mode explained that fragment growth contributed to larger ligands, leading to improved suitability at the docking pocket. In the way of fragment growth, the larger side chain with extensive contact at terminal is obviously better than substituted benzene ring. The enhancement of docking activity is mainly due to the new fragments such as alkyl chains and rings with amino groups at NVP terminal, resulting in a large increase in hydrophobic bonding and the new addition of hydrogen bonding or salt bonding. This study is expected to provide reference for the research on non-nucleoside reverse transcriptase inhibitors resistance and AIDS treatment.

Indexed as

Anti-HIV AgentsNevirapineBinding SitesDrug DesignHIV Reverse TranscriptaseLigandsMolecular Docking SimulationMutant ProteinsReverse Transcriptase InhibitorsAnti-HIV AgentsHIV Reverse TranscriptaseLigandsMutant ProteinsNevirapinereverse transcriptase, Human immunodeficiency virus 1Reverse Transcriptase Inhibitorsfragment growthHIV-1molecular dockingnevirapineY188C mutation HIV-1 reverse transcriptase

Identifiers

PMID36364174

DOI10.3390/molecules27217348

PMCPMC9659058

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.