{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Jimenez-Avalos G"],"funding":["Consejo Nacional de Ciencia, Tecnología e Innovación Tecnológica"],"pagination":["15452"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8322093"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11(1)"],"pubmed_abstract":["SARS-CoV-2 main protease is a common target for inhibition assays due to its high conservation among coronaviruses. Since flavonoids show antiviral activity, several in silico works have proposed them as potential SARS-CoV-2 main protease inhibitors. Nonetheless, there is reason to doubt certain results given the lack of consideration for flavonoid promiscuity or main protease plasticity, usage of short library sizes, absence of control molecules and/or the limitation of the methodology to a single target site. Here, we report a virtual screening study where dorsilurin E, euchrenone a11, sanggenol O and CHEMBL2171598 are proposed to inhibit main protease through different pathways. Remarkably, novel structural mechanisms were observed after sanggenol O and CHEMBL2171598 bound to experiment"],"journal":["Scientific reports"],"pubmed_title":["Comprehensive virtual screening of 4.8 k flavonoids reveals novel insights into allosteric inhibition of SARS-CoV-2 M<sup>PRO</sup>."],"pmcid":["PMC8322093"],"funding_grant_id":["048-2020"],"pubmed_authors":["Guevara-Sarmiento L","Calderon K","Delgado-Ccancce E","Perez-M N","Zimic M","Choque-Guevara R","Salguedo-Bohorquez MI","Fernandez-Sanchez M","Gutierrez K","Criollo-Orozco M","De La Cruz L","Ramirez-Ortiz I","Licla-Inca A","Icochea E","Tataje-Lavanda L","Vallejos-Sanchez K","Juscamaita-Bartra RA","Romero YK","Ygnacio-Aguirre F","Villanueva-Perez D","Antiparra R","Elugo-Guevara C","Jimenez-Avalos G","de Grecia Cauti-Mendoza M","Huerta-Roque P","Heredia-Almeyda O","Chunga-Giron X","Fernandez-Diaz M","Rios-Matos D","Ticona J","Olivos-Ramirez GE","Rojas-Neyra A","Ochoa-Ortiz A","Poma-Acevedo A","Agurto-Arteaga A","Quiliano M","Pauyac K","Quinones-Garcia S","Sernaque-Aguilar Y","COVID-19 Working Group in Perú","Ardiles-Reyes M","Soto LF","Cauna-Orocollo Y","Delgado-Pease NE","Huaccachi-Gonzalez E","Vargas-Ruiz AP","Rios-Angulo AA","Sheen P","Isasi-Rivas G","Paucar-Montoro E","Chipana-Flores N","Montalvan A","Montesinos-Millan R","Nunez-Fernandez D","Perez-Martinez JL","Ramos-Sono D"],"additional_accession":[]},"is_claimable":false,"name":"Comprehensive virtual screening of 4.8 k flavonoids reveals novel insights into allosteric inhibition of SARS-CoV-2 M<sup>PRO</sup>.","description":"SARS-CoV-2 main protease is a common target for inhibition assays due to its high conservation among coronaviruses. Since flavonoids show antiviral activity, several in silico works have proposed them as potential SARS-CoV-2 main protease inhibitors. Nonetheless, there is reason to doubt certain results given the lack of consideration for flavonoid promiscuity or main protease plasticity, usage of short library sizes, absence of control molecules and/or the limitation of the methodology to a single target site. Here, we report a virtual screening study where dorsilurin E, euchrenone a11, sanggenol O and CHEMBL2171598 are proposed to inhibit main protease through different pathways. Remarkably, novel structural mechanisms were observed after sanggenol O and CHEMBL2171598 bound to experiment","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Jul","modification":"2026-05-08T12:02:04.728Z","creation":"2025-05-29T20:55:45.218Z"},"accession":"S-EPMC8322093","cross_references":{"pubmed":["34326429"],"doi":["10.1038/s41598-021-94951-6"]}}