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This study presents the synthesis and detailed characterization of six novel Schiff base sulfonate derivatives (\n                    <jats:bold>\n                      L\n                      <jats:sup>1<\/jats:sup>\n                      \u2013L\n                      <jats:sup>6<\/jats:sup>\n                    <\/jats:bold>\n                    ) through spectroscopic techniques (FT\u2010IR and NMR). Their inhibitory potential was evaluated against human carbonic anhydrase isoenzymes (\n                    <jats:italic>h<\/jats:italic>\n                    CA I and\n                    <jats:italic>h<\/jats:italic>\n                    CA II) and acetylcholinesterase (AChE), which are crucial therapeutic targets for diseases such as glaucoma, epilepsy, and Alzheimer's disease. The\n                    <jats:italic>K<\/jats:italic>\n                    <jats:sub>I<\/jats:sub>\n                    values for the compounds concerning AChE,\n                    <jats:italic>h<\/jats:italic>\n                    CA I, and\n                    <jats:italic>h<\/jats:italic>\n                    CA II enzymes were in the ranges of 106.10\u00a0\u00b1\u00a014.73 to 422.80\u00a0\u00b1\u00a017.64\u00a0nM (THA: 159.61\u00a0\u00b1\u00a08.41\u00a0nM), 116.90\u00a0\u00b1\u00a024.40 to 268.00\u00a0\u00b1\u00a035.84\u00a0nM (AAZ: 439.17\u00a0\u00b1\u00a09.30\u00a0nM), and 177.00\u00a0\u00b1\u00a035.03 to 435.20\u00a0\u00b1\u00a075.98\u00a0nM (AAZ: 98.28\u00a0\u00b1\u00a01.69\u00a0nM), respectively. Molecular docking analyses revealed key interactions within the active sites of the enzymes, including hydrogen bonding with critical residues and \u03c0\u2013\u03c0 stacking interactions. Notably,\n                    <jats:bold>\n                      L\n                      <jats:sup>3<\/jats:sup>\n                    <\/jats:bold>\n                    demonstrated superior inhibition against\n                    <jats:italic>h<\/jats:italic>\n                    CA I (\n                    <jats:italic>K<\/jats:italic>\n                    <jats:sub>I<\/jats:sub>\n                    : 116.90\u00a0\u00b1\u00a024.40\u00a0nM) and AChE (\n                    <jats:italic>K<\/jats:italic>\n                    <jats:sub>I<\/jats:sub>\n                    : 106.10\u00a0\u00b1\u00a014.73\u00a0nM), positioning it as a promising lead compound. This comprehensive investigation contributes to the development of isoform\u2010specific inhibitors for therapeutic use and provides valuable insights into their binding mechanisms. The findings underscore the potential of Schiff base sulfonates as scaffolds in drug discovery for neurodegenerative and metabolic disorders.\n                  <\/jats:p>","DOI":"10.1002\/cbdv.202402893","type":"journal-article","created":{"date-parts":[[2024,12,10]],"date-time":"2024-12-10T01:55:05Z","timestamp":1733795705000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":14,"title":["Novel Schiff Base Sulfonate Derivatives as Carbonic Anhydrase and Acetylcholinesterase Inhibitors: Synthesis, Biological Activity, and Molecular Docking Insights"],"prefix":"10.1002","volume":"22","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-8110-7747","authenticated-orcid":false,"given":"\u00dcmit","family":"Ya\u015far","sequence":"first","affiliation":[{"name":"Department of Laboratory and Veterinary Health, Nihat Delibalta G\u00f6le Vocational High School Ardahan University  Ardahan 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