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SARS-CoV-2 Main Protease Active Site Ligands in the Human Metabolome
In late 2019, a global pandemic occurred. The causative agent was identified as a member of the Coronaviridae family, called severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). In this study, we present an analysis on the substances identified in the human metabolome capable of binding the...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7961382/ https://www.ncbi.nlm.nih.gov/pubmed/33807773 http://dx.doi.org/10.3390/molecules26051409 |
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author | Sardanelli, Anna Maria Isgrò, Camilla Palese, Luigi Leonardo |
author_facet | Sardanelli, Anna Maria Isgrò, Camilla Palese, Luigi Leonardo |
author_sort | Sardanelli, Anna Maria |
collection | PubMed |
description | In late 2019, a global pandemic occurred. The causative agent was identified as a member of the Coronaviridae family, called severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). In this study, we present an analysis on the substances identified in the human metabolome capable of binding the active site of the SARS-CoV-2 main protease (M(pro)). The substances present in the human metabolome have both endogenous and exogenous origins. The aim of this research was to find molecules whose biochemical and toxicological profile was known that could be the starting point for the development of antiviral therapies. Our analysis revealed numerous metabolites—including xenobiotics—that bind this protease, which are essential to the lifecycle of the virus. Among these substances, silybin, a flavolignan compound and the main active component of silymarin, is particularly noteworthy. Silymarin is a standardized extract of milk thistle, Silybum marianum, and has been shown to exhibit antioxidant, hepatoprotective, antineoplastic, and antiviral activities. Our results—obtained in silico and in vitro—prove that silybin and silymarin, respectively, are able to inhibit M(pro), representing a possible food-derived natural compound that is useful as a therapeutic strategy against COVID-19. |
format | Online Article Text |
id | pubmed-7961382 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-79613822021-03-17 SARS-CoV-2 Main Protease Active Site Ligands in the Human Metabolome Sardanelli, Anna Maria Isgrò, Camilla Palese, Luigi Leonardo Molecules Article In late 2019, a global pandemic occurred. The causative agent was identified as a member of the Coronaviridae family, called severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). In this study, we present an analysis on the substances identified in the human metabolome capable of binding the active site of the SARS-CoV-2 main protease (M(pro)). The substances present in the human metabolome have both endogenous and exogenous origins. The aim of this research was to find molecules whose biochemical and toxicological profile was known that could be the starting point for the development of antiviral therapies. Our analysis revealed numerous metabolites—including xenobiotics—that bind this protease, which are essential to the lifecycle of the virus. Among these substances, silybin, a flavolignan compound and the main active component of silymarin, is particularly noteworthy. Silymarin is a standardized extract of milk thistle, Silybum marianum, and has been shown to exhibit antioxidant, hepatoprotective, antineoplastic, and antiviral activities. Our results—obtained in silico and in vitro—prove that silybin and silymarin, respectively, are able to inhibit M(pro), representing a possible food-derived natural compound that is useful as a therapeutic strategy against COVID-19. MDPI 2021-03-05 /pmc/articles/PMC7961382/ /pubmed/33807773 http://dx.doi.org/10.3390/molecules26051409 Text en © 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Sardanelli, Anna Maria Isgrò, Camilla Palese, Luigi Leonardo SARS-CoV-2 Main Protease Active Site Ligands in the Human Metabolome |
title | SARS-CoV-2 Main Protease Active Site Ligands in the Human Metabolome |
title_full | SARS-CoV-2 Main Protease Active Site Ligands in the Human Metabolome |
title_fullStr | SARS-CoV-2 Main Protease Active Site Ligands in the Human Metabolome |
title_full_unstemmed | SARS-CoV-2 Main Protease Active Site Ligands in the Human Metabolome |
title_short | SARS-CoV-2 Main Protease Active Site Ligands in the Human Metabolome |
title_sort | sars-cov-2 main protease active site ligands in the human metabolome |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7961382/ https://www.ncbi.nlm.nih.gov/pubmed/33807773 http://dx.doi.org/10.3390/molecules26051409 |
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