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To investigate potential strategies for restoring \u03b2\u2010lactam activity, a panel of compounds was evaluated as putative MBL inhibitors and antibiotic adjuvants. The panel included FDA\u2010approved drugs (carbonic anhydrase inhibitors, an antiviral agent, and a metal chelator), and two novel histidine\u2013pyridine derivatives (D\u2010 and L\u20102\u2010amino\u20103\u2010(1H\u2010imidazol\u20104\u2010yl)\u2010N\u2010[2\u2010(pyridin\u20102\u2010yl)ethyl]propenamides). The latter were synthesized and characterized by NMR spectroscopy and mass spectrometry. Combination assays against Verona Integron\u2013encoded Metallo\u2010\u03b2\u2010Lactamase 1 (VIM\u20101)\u2013producing\n                    <jats:italic>Klebsiella pneumoniae<\/jats:italic>\n                    showed that D\u2010penicillamine and chlorpropamide restored meropenem activity. These effects were supported by time\u2010dependent inhibition and checkerboard assays. Molecular docking and MD simulations with the VIM\u20101 enzyme further elucidated the putative binding modes of these inhibitors. These results suggest that\u00a0repurposing the conventional D\u2010penicillamine and chlorpropamide drugs can effectively counteract MBL\u2010mediated resistance.\n                  <\/jats:p>","DOI":"10.1002\/cbic.70509","type":"journal-article","created":{"date-parts":[[2026,8,26]],"date-time":"2026-08-26T12:54:02Z","timestamp":1787748842000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Restoring Meropenem Activity Against VIM\u20101\u2010Producing\n                    <i>Klebsiella<\/i>\n                    <i>pneumoniae<\/i>\n                    Through Zinc\u2010Binding Ligands"],"prefix":"10.1002","volume":"27","author":[{"ORCID":"https:\/\/orcid.org\/0009-0003-6822-481X","authenticated-orcid":false,"given":"Chiara","family":"Ragusa","sequence":"first","affiliation":[{"name":"Dipartimento di Scienze Chimiche Universit\u00e0 degli Studi di Catania  Catania 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