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The burden on healthcare systems around the world has been reduced by the success of vaccines. However, population adherence and the occurrence of severe acute respiratory syndrome coronavirus 2 (SARS\u2010CoV\u20102) variants are still challenging tasks to be affronted. In addition, the newly approved drug presents some limitations in terms of side effects and drug interference, highlighting the importance of searching for new antiviral agents against SARS\u2010CoV\u20102. The SARS\u2010CoV\u20102 main protease (M\n                    <jats:sup>pr<\/jats:sup>\n                    <jats:sup>o<\/jats:sup>\n                    ) represents a versatile target to search for new drug candidates due to its essential role in proteolytic activities responsible for the virus replication. In this work, a series of 190 compounds, composed of 27 natural ones and 163 synthetic compounds, were screened in vitro for their inhibitory effects against SARS\u2010CoV\u20102 M\n                    <jats:sup>pro<\/jats:sup>\n                    . Twenty\u2010five compounds inhibited M\n                    <jats:sup>pro<\/jats:sup>\n                    with inhibitory constant values (\n                    <jats:italic>K<\/jats:italic>\n                    <jats:sub>i<\/jats:sub>\n                    ) between 23.2 and 241\u2009\u00b5M. Among them, a thiosemicarbazone derivative was the most active compound. Molecular docking studies using Protein Data Bank ID 5RG1, 5RG2, and 5RG3 crystal structures of M\n                    <jats:sup>pro<\/jats:sup>\n                    revealed important interactions identified as hydrophobic, hydrogen bonding and steric interactions with amino acid residues in the active site cavity. Overall, our findings indicate the described thiosemicarbazones as good candidates to be further explored to develop antiviral leads against SARS\u2010CoV\u20102. Moreover, the studies showed the importance of careful evaluation of test results to detect and exclude false\u2010positive findings.\n                  <\/jats:p>","DOI":"10.1002\/ardp.202300207","type":"journal-article","created":{"date-parts":[[2023,5,31]],"date-time":"2023-05-31T09:44:55Z","timestamp":1685526295000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Inhibitory effects of 190 compounds against SARS\u2010CoV\u20102 M\n                    <sup>pr<\/sup>\n                    <sup>o<\/sup>\n                    protein: Molecular docking interactions"],"prefix":"10.1002","volume":"356","author":[{"given":"Gabriella B.","family":"Souza","sequence":"first","affiliation":[{"name":"Department of Chemistry, CFM Universidade Federal de Santa Catarina, Campus Universit\u00e1rio\u2010Trindade Florian\u00f3polis Santa Catarina Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2404-3817","authenticated-orcid":false,"given":"Larissa","family":"Sens","sequence":"additional","affiliation":[{"name":"Department of Chemistry, CFM Universidade Federal de Santa Catarina, Campus Universit\u00e1rio\u2010Trindade Florian\u00f3polis Santa Catarina Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0769-8435","authenticated-orcid":false,"given":"Stefan J.","family":"Hammerschmidt","sequence":"additional","affiliation":[{"name":"Institute of Pharmaceutical and Biomedical Sciences, Johannes Gutenberg\u2010University of Mainz Mainz Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7131-6414","authenticated-orcid":false,"given":"Nat\u00e1lia F.","family":"de Sousa","sequence":"additional","affiliation":[{"name":"Chemistry Department, Exact and Nature Sciences Center Federal University of Paraiba, Campus I Jo\u00e3o Pessoa Para\u00edba Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maryelle A. 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