Dublin Core The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/. Title A name given to the resource Articles Article Faculty Publications -Articles Dublin Core The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/. Title A name given to the resource Computational screening of natural compounds from Salvia plebeia R. Br. for inhibition of SARS-CoV-2 main protease Subject The topic of the resource ADMET; Main protease; Molecular docking; Molecular dynamic simulation; PASS; Plebeiosides B; Rutin; Salvia plebeia R. Br Description An account of the resource The novel Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV-2) has emerged to be the reason behind the COVID-19 pandemic. It was discovered in Wuhan, China and then began spreading around the world, impacting the health of millions. Efforts for treatment have been hampered as there are no antiviral drugs that are effective against this virus. In the present study, we have explored the phytochemical constituents of Salvia plebeia R. Br., in terms of its binding affinity by targeting COVID-19 main protease (Mpro) using computational analysis. Molecular docking analysis was performed using PyRx software. The ADMET and drug-likeness properties of the top 10 compounds showing binding affinity greater than or equal to ? 8.0kcal/mol were analysed using pkCSM and DruLiTo, respectively. Based on the docking studies, it was confirmed that Rutin and Plebeiosides B were the most potent inhibitors of the main protease of SARS-CoV-2 with the best binding affinities of ? 9.1kcal/mol and ? 8.9kcal/mol, respectively. Further, the two compounds were analysed by studying their biological activity using the PASS webserver. Molecular dynamics simulation analysis was performed for the selected proteinligand complexes to confirm their stability at 300ns. MM-PBSA provided the basis for analyzing the affinity of the phytochemicals towards Mpro by calculating the binding energy, and secondary structure analysis indicated the stability of protease structure when it is bound to Rutin and Plebeiosides B. Altogether, the study identifies Rutin and Plebeiosides B to be potent Mpro inhibitors of SARS-CoV-2. Graphic abstract: [Figure not available: see fulltext.] 2021, Society for Plant Research. Creator An entity primarily responsible for making the resource Zackria A.A.; Pattabiraman R.; Murthy T.P.K.; Kumar S.B.; Mathew B.B.; Biju V.G. Source A related resource from which the described resource is derived Vegetos, Vol-35, No. 2, pp. 345-359. Publisher An entity responsible for making the resource available Springer Date A point or period of time associated with an event in the lifecycle of the resource 2022-01-01 Identifier An unambiguous reference to the resource within a given context <a href="https://doi.org/10.1007/s42535-021-00304-z" target="_blank" rel="noreferrer noopener">https://doi.org/10.1007/s42535-021-00304-z</a> <br /><br /><a href="https://www.scopus.com/inward/record.uri?eid=2-s2.0-85117313884&amp;doi=10.1007%2Fs42535-021-00304-z&amp;partnerID=40&amp;md5=547a75b74071a11893d6a340c6346703" target="_blank" rel="noreferrer noopener">https://www.scopus.com/inward/record.uri?eid=2-s2.0-85117313884&amp;doi=10.1007%2fs42535-021-00304-z&amp;partnerID=40&amp;md5=547a75b74071a11893d6a340c6346703</a> Rights Information about rights held in and over the resource All Open Access; Green Open Access; Hybrid Gold Open Access Relation A related resource ISSN: 9704078 Format The file format, physical medium, or dimensions of the resource Online Language A language of the resource English Type The nature or genre of the resource Article Coverage The spatial or temporal topic of the resource, the spatial applicability of the resource, or the jurisdiction under which the resource is relevant Zackria A.A., Department of Biotechnology, M S Ramaiah Institute of Technology, Karnataka, Bengaluru, 560054, India; Pattabiraman R., Department of Biotechnology, M S Ramaiah Institute of Technology, Karnataka, Bengaluru, 560054, India; Murthy T.P.K., Department of Biotechnology, M S Ramaiah Institute of Technology, Karnataka, Bengaluru, 560054, India; Kumar S.B., Department of Biotechnology, M S Ramaiah Institute of Technology, Karnataka, Bengaluru, 560054, India; Mathew B.B., Department of Biotechnology, Dayananda Sagar College of Engineering, Karnataka, Bengaluru, 560078, India; Biju V.G., Department of Computer Science and Engineering, Christ (Deemed-to-be University), Karnataka, Bengaluru, 560060, India