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Comparative study of the interaction of ivermectin with proteins of interest associated with SARS-CoV-2: A computational and biophysical approach
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...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier B.V.
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8373590/ https://www.ncbi.nlm.nih.gov/pubmed/34428682 http://dx.doi.org/10.1016/j.bpc.2021.106677 |
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author | González-Paz, Lenin Hurtado-León, María Laura Lossada, Carla Fernández-Materán, Francelys V. Vera-Villalobos, Joan Loroño, Marcos Paz, J.L. Jeffreys, Laura Alvarado, Ysaias J. |
author_facet | González-Paz, Lenin Hurtado-León, María Laura Lossada, Carla Fernández-Materán, Francelys V. Vera-Villalobos, Joan Loroño, Marcos Paz, J.L. Jeffreys, Laura Alvarado, Ysaias J. |
author_sort | González-Paz, Lenin |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-8373590 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Elsevier B.V. |
record_format | MEDLINE/PubMed |
spelling | pubmed-83735902021-08-19 Comparative study of the interaction of ivermectin with proteins of interest associated with SARS-CoV-2: A computational and biophysical approach González-Paz, Lenin Hurtado-León, María Laura Lossada, Carla Fernández-Materán, Francelys V. Vera-Villalobos, Joan Loroño, Marcos Paz, J.L. Jeffreys, Laura Alvarado, Ysaias J. Biophys Chem Article 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. Elsevier B.V. 2021-11 2021-08-19 /pmc/articles/PMC8373590/ /pubmed/34428682 http://dx.doi.org/10.1016/j.bpc.2021.106677 Text en © 2021 Elsevier B.V. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active. |
spellingShingle | Article González-Paz, Lenin Hurtado-León, María Laura Lossada, Carla Fernández-Materán, Francelys V. Vera-Villalobos, Joan Loroño, Marcos Paz, J.L. Jeffreys, Laura Alvarado, Ysaias J. Comparative study of the interaction of ivermectin with proteins of interest associated with SARS-CoV-2: A computational and biophysical approach |
title | Comparative study of the interaction of ivermectin with proteins of interest associated with SARS-CoV-2: A computational and biophysical approach |
title_full | Comparative study of the interaction of ivermectin with proteins of interest associated with SARS-CoV-2: A computational and biophysical approach |
title_fullStr | Comparative study of the interaction of ivermectin with proteins of interest associated with SARS-CoV-2: A computational and biophysical approach |
title_full_unstemmed | Comparative study of the interaction of ivermectin with proteins of interest associated with SARS-CoV-2: A computational and biophysical approach |
title_short | Comparative study of the interaction of ivermectin with proteins of interest associated with SARS-CoV-2: A computational and biophysical approach |
title_sort | comparative study of the interaction of ivermectin with proteins of interest associated with sars-cov-2: a computational and biophysical approach |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8373590/ https://www.ncbi.nlm.nih.gov/pubmed/34428682 http://dx.doi.org/10.1016/j.bpc.2021.106677 |
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