Comparative study of the interaction of ivermectin with proteins of interest associated with SARS-CoV-2: A computational and biophysical approach

Lenin González-Paz, María Laura Hurtado-León, Carla Lossada, Francelys V. Fernández-Materán, Joan Vera-Villalobos, Marcos Loroño, J. L. Paz, Laura Jeffreys, Ysaias J. Alvarado

Research output: Contribution to journalArticlepeer-review

Abstract

The SARS-CoV-2 pandemic has accelerated the study of existing drugs. The mixture of homologs called ivermectin (avermectin-B1a [HB1a] + avermectin-B1b [HB1b]) has shown antiviral activity against SARS-CoV-2 in vitro. However, there are few reports on the behavior of each homolog. We investigated the interaction of each homolog with promising targets of interest associated with SARS-CoV-2 infection from a biophysical and computational-chemistry perspective using docking and molecular dynamics. We observed a differential behavior for each homolog, with an affinity of HB1b for viral structures, and of HB1a for host structures considered. The induced disturbances were differential and influenced by the hydrophobicity of each homolog and of the binding pockets. We present the first comparative analysis of the potential theoretical inhibitory effect of both avermectins on biomolecules associated with COVID-19, and suggest that ivermectin through its homologs, has a multiobjective behavior.

Original languageEnglish
Article number106677
JournalBiophysical Chemistry
Volume278
DOIs
StatePublished - Nov 2021

Bibliographical note

Publisher Copyright:
© 2021 Elsevier B.V.

Keywords

  • Avermectin
  • COVID-19
  • Ivermectin
  • Molecular docking
  • Molecular dynamic
  • SARS-CoV-2

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