Discovery of a Novel HIV-1 Integrase/p75 Interacting Inhibitor by Docking Screening, Biochemical Assay, and in Vitro Studies

J Chem Inf Model. 2017 Sep 25;57(9):2336-2343. doi: 10.1021/acs.jcim.7b00402. Epub 2017 Sep 11.

Abstract

Protein-protein interaction between lens epithelium-derived growth factor (LEDGF/p75) and HIV-1 integrase becomes an attractive target for anti-HIV drug development. The blockade of this interaction by small molecules could potentially inhibit HIV-1 replication. These small molecules are termed as LEDGINs; and several newly identified LEDGINs have been reported to significantly reduce HIV-1 replication. Through this project, we have finished the docking screening of the Maybridge database against the p75 binding site of HIV-1 integrase using both DOCK and Autodock Vina software. Finally, we have successfully identified a novel scaffold LEDGINs inhibitor DW-D-5. Its antiviral activities and anticatalytic activity of HIV-1 integrase are similar to other LEDGINs under development. We demonstrated that the combination of DW-D-5 and FDA approved anti-HIV drugs resulted in additive inhibitory effects on HIV-1 replication, indicating that DW-D-5 could be an important component of combination pills for clinic use in HIV treatment.

MeSH terms

  • Anti-HIV Agents / metabolism
  • Anti-HIV Agents / pharmacology*
  • Biocatalysis
  • Cell Line
  • Drug Evaluation, Preclinical / methods*
  • HIV Integrase / chemistry
  • HIV Integrase / metabolism*
  • HIV-1 / drug effects
  • HIV-1 / metabolism
  • HIV-1 / physiology
  • Intercellular Signaling Peptides and Proteins / chemistry
  • Intercellular Signaling Peptides and Proteins / metabolism*
  • Molecular Docking Simulation
  • Protein Binding
  • Protein Conformation
  • Software
  • Virus Replication / drug effects

Substances

  • Anti-HIV Agents
  • Intercellular Signaling Peptides and Proteins
  • lens epithelium-derived growth factor
  • HIV Integrase
  • p31 integrase protein, Human immunodeficiency virus 1