Anti-HIV-1 integrase potency of methylgallate from Alchornea cordifolia using in vitro and in silico approaches

Sci Rep. 2019 Mar 18;9(1):4718. doi: 10.1038/s41598-019-41403-x.

Abstract

According to the 2018 report of the United Nations Programme on HIV/AIDS (UNAIDS), acquired immune deficiency syndrome (AIDS), a disease caused by the human immunodeficiency virus (HIV), remains a significant public health problem. The non-existence of a cure or effective vaccine for the disease and the associated emergence of resistant viral strains imply an urgent need for the discovery of novel anti-HIV drug candidates. The current study aimed to identify potential anti-retroviral compounds from Alchornea cordifolia. Bioactive compounds were identified using several chromatographic and spectroscopic techniques and subsequently evaluated for cytotoxicity and anti-HIV properties. Molecular modelling studies against HIV-1 integrase (HIV-1 IN) were performed to decipher the mode of action of methylgallate, the most potent compound (IC50 = 3.7 nM) and its analogues from ZINC database. Cytotoxicity assays showed that neither the isolated compounds nor the crude methanolic extract displayed cytotoxicity effects on the HeLa cell line. A strong correlation between the in vitro and in silico results was observed and important HIV-1 IN residues interacting with the different compounds were identified. These current results indicate that methylgallate is the main anti-HIV-1 compound in A. cordifolia stem bark, and could be a potential platform for the development of new HIV-1 IN inhibitors.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acquired Immunodeficiency Syndrome / drug therapy*
  • Acquired Immunodeficiency Syndrome / virology
  • Drug Evaluation, Preclinical
  • Euphorbiaceae / chemistry*
  • Gallic Acid / analogs & derivatives*
  • Gallic Acid / chemistry
  • Gallic Acid / isolation & purification
  • Gallic Acid / pharmacology
  • Gallic Acid / therapeutic use
  • HIV Integrase / metabolism*
  • HIV Integrase / ultrastructure
  • HIV Integrase Inhibitors / chemistry
  • HIV Integrase Inhibitors / isolation & purification
  • HIV Integrase Inhibitors / pharmacology*
  • HIV Integrase Inhibitors / therapeutic use
  • HIV-1 / drug effects
  • HIV-1 / enzymology
  • HeLa Cells
  • Humans
  • Inhibitory Concentration 50
  • Molecular Docking Simulation
  • Molecular Dynamics Simulation
  • Plant Bark / chemistry
  • Plant Stems / chemistry
  • Protein Domains
  • Recombinant Proteins
  • Toxicity Tests

Substances

  • HIV Integrase Inhibitors
  • Recombinant Proteins
  • methyl gallate
  • Gallic Acid
  • HIV Integrase
  • p31 integrase protein, Human immunodeficiency virus 1