{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,9]],"date-time":"2026-01-09T14:40:20Z","timestamp":1767969620459,"version":"3.49.0"},"reference-count":48,"publisher":"Wiley","issue":"7","license":[{"start":{"date-parts":[[2025,7,23]],"date-time":"2025-07-23T00:00:00Z","timestamp":1753228800000},"content-version":"vor","delay-in-days":22,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Archiv der Pharmazie"],"published-print":{"date-parts":[[2025,7]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    A thiourea series (\n                    <jats:bold>7a\u2013l<\/jats:bold>\n                    ) containing 4\u2010arylthiazoles and the\n                    <jats:sc>d<\/jats:sc>\n                    \u2010galactose moiety were synthesized and explored for their multi\u2010target inhibition against \u03b1\n                    <jats:italic>\u2010<\/jats:italic>\n                    amylase from porcine pancreas and \u03b1\n                    <jats:italic>\u2010<\/jats:italic>\n                    glucosidase from\n                    <jats:italic>Saccharomyces cerevisiae<\/jats:italic>\n                    . Among these thioureas,\n                    <jats:bold>7h<\/jats:bold>\n                    was the most potent inhibitor for \u03b1\u2010amylase (IC\n                    <jats:sub>50<\/jats:sub>\n                    of 7.84\u2009\u00b1\u20090.14\u2009\u03bcM) and\n                    <jats:bold>7c<\/jats:bold>\n                    was the most potent inhibitor for \u03b1\u2010glucosidase (IC\n                    <jats:sub>50<\/jats:sub>\n                    of 7.15\u2009\u00b1\u20090.12\u2009\u03bcM). These thioureas also exhibited anti\u2010glycation and antioxidant activity. They were noncytotoxic for NIH\u20103T3 cells. Induced\u2010fit molecular docking study was applied to the two most potential inhibitors\n                    <jats:bold>7c<\/jats:bold>\n                    and\n                    <jats:bold>7h<\/jats:bold>\n                    . Their active interactions with residues in the catalytic pockets of the corresponding studied enzymes, 1OSE and 3TOP, were suitable to their inhibitory potentials against each tested enzyme. The molecular dynamics simulations validated the in vitro data for these compounds whereas the pharmacokinetics profile (ADMET) revealed the druglike properties of potent inhibitors.\n                  <\/jats:p>","DOI":"10.1002\/ardp.70039","type":"journal-article","created":{"date-parts":[[2025,7,24]],"date-time":"2025-07-24T06:31:37Z","timestamp":1753338697000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Substituted\n                    <scp>D<\/scp>\n                    \u2010Galactose\u2010Conjugated Thiazole\u2010Thioureas Derivatives as Promising Antidiabetic Agents: Synthesis, In Vitro Inhibition, and Molecular Simulation for \u03b1\u2010Amylase, \u03b1\u2010Glucosidase, Protein Glycation, and Oxidative Stress"],"prefix":"10.1002","volume":"358","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-2267-1775","authenticated-orcid":false,"given":"Nguyen 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