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Related Experiment Video

Updated: Aug 3, 2025

Rapid Screening of HIV Reverse Transcriptase and Integrase Inhibitors

Rapid Screening of HIV Reverse Transcriptase and Integrase Inhibitors

Published on: April 9, 2014

Targeting HIV-1 Reverse Transcriptase Using a Fragment-Based Approach.

Mahta Mansouri¹, Shawn Rumrill², Shane Dawson¹

¹Medicinal Chemistry, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, VIC 3052, Australia.

Molecules (Basel, Switzerland)

|April 13, 2023

Summary

This summary is machine-generated.

Researchers optimized a fragment to inhibit HIV-1 replication by targeting reverse transcriptase (RT). A novel compound was developed, offering a new strategy for dual-site inhibitors against drug-resistant HIV-1.

Keywords:

HIV-1 drug discovery fragment-based drug design non-nucleoside reverse transcriptase inhibitors (NNRTIs)reverse transcriptase

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Determining 3'-Termini and Sequences of Nascent Single-Stranded Viral DNA Molecules during HIV-1 Reverse Transcription in Infected Cells

Determining 3'-Termini and Sequences of Nascent Single-Stranded Viral DNA Molecules during HIV-1 Reverse Transcription in Infected Cells

Published on: January 30, 2019

Area of Science:

Virology
Medicinal Chemistry
Drug Discovery

Background:

Human immunodeficiency virus type I (HIV-1) infection leads to acquired immunodeficiency syndrome (AIDS) and remains a global health challenge.
Emergence of drug-resistant HIV-1 strains necessitates the development of novel antiviral agents targeting new pathways.
HIV-1 reverse transcriptase (RT) is a critical enzyme in viral replication and a target for existing antiretroviral therapies.

Purpose of the Study:

To optimize a previously identified fragment (compound B-1) that binds to HIV-1 RT at a novel site.
To synthesize and evaluate novel compounds for improved HIV-1 RT inhibition and binding.
To explore the development of dual inhibitors targeting both the NNRTI-binding pocket (NNIBP) and an adjacent site.

Main Methods:

Fragment-based drug discovery approach was employed.
Three series of compounds were synthesized and characterized.
In vitro assays were conducted to assess HIV-1 RT binding and inhibitory activity.

Main Results:

The 4-position of the core scaffold was identified as crucial for fragment binding to HIV-1 RT.
A lead compound, 27, featuring a cyclopropyl substitution, demonstrated significant inhibitory activity.
Compound 27 functions as a minimal yet efficient non-nucleoside reverse transcriptase inhibitor (NNRTI).

Conclusions:

Optimization of fragment B-1 led to the identification of potent HIV-1 RT inhibitors.
The study identified key structural requirements for binding to both the NNIBP and an adjacent site.
Lead compound 27 serves as a promising starting point for developing novel dual NNIBP-Adjacent site inhibitors against HIV-1.