Elsevier

Biophysical Chemistry

Volume 278, November 2021, 106677
Biophysical Chemistry

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

https://doi.org/10.1016/j.bpc.2021.106677Get rights and content

Highlights

  • Each ivermectin homolog stably binds to the tested proteins.

  • An affinity of avermectin B1b for viral proteins, and avermectin B1a for cellular proteins was identified.

  • The inhibition kinetics was influenced by the hydrophobicity of the proteins and by the chemical groups of each homolog.

  • The behavior of each homolog could contribute to the possible reported activity of ivermectin on multiple targets.

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.

Keywords

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

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