Covalently Targeted Highly Conserved Tyr318 to Improve the Drug Resistance Profiles of HIV-1 NNRTIs: A Proof-of-Concept Study

Int J Mol Sci. 2023 Jan 7;24(2):1215. doi: 10.3390/ijms24021215.

Abstract

This study presents proof of concept for designing a novel HIV-1 covalent inhibitor targeting the highly conserved Tyr318 in the HIV-1 non-nucleoside reverse transcriptase inhibitors binding pocket to improve the drug resistance profiles. The target inhibitor ZA-2 with a fluorosulfate warhead in the structure was found to be a potent inhibitor (EC50 = 11-246 nM) against HIV-1 IIIB and a panel of NNRTIs-resistant strains, being far superior to those of NVP and EFV. Moreover, ZA-2 was demonstrated with lower cytotoxicity (CC50 = 125 µM). In the reverse transcriptase inhibitory assay, ZA-2 exhibited an IC50 value of 0.057 µM with the ELISA method, and the MALDI-TOF MS data demonstrated the covalent binding mode of ZA-2 with the enzyme. Additionally, the molecular simulations have also demonstrated that compounds can form covalent binding to the Tyr318.

Keywords: DAPYs; HIV-1; NNRTIs; covalent inhibitors; drug resistance.

MeSH terms

  • Anti-HIV Agents* / chemistry
  • Anti-HIV Agents* / pharmacology
  • Drug Design
  • HIV Reverse Transcriptase / metabolism
  • HIV-1* / metabolism
  • Reverse Transcriptase Inhibitors / chemistry
  • Reverse Transcriptase Inhibitors / pharmacology
  • Structure-Activity Relationship

Substances

  • Reverse Transcriptase Inhibitors
  • Anti-HIV Agents
  • HIV Reverse Transcriptase