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The chemical structures of new hybrids were confirmed by elemental analysis and some spectroscopic techniques. All tested compounds showed low nanomolar inhibition with IC\n                    <jats:sub>50<\/jats:sub>\n                    values of in the range of 30.4\u2013264.0\u2005nM against hCA I, 23.2\u2013251.6\u2005nM against hCA II, 12.1\u2013114.3\u2005nM against AChE, and 76.4\u2013134.0\u2005nM against BChE. These compounds inhibited hCA I and AChE more than acetazolamide (AZA) and neostigmine. Among them, compounds\n                    <jats:bold>2c<\/jats:bold>\n                    and\n                    <jats:bold>2e<\/jats:bold>\n                    , which have a linear structure, were determined to be the most active inhibitor candidates against these selected enzymes. Molecular docking studies were carried out on the compounds (\n                    <jats:bold>2a\u2010<\/jats:bold>\n                    \u2010\n                    <jats:bold>g<\/jats:bold>\n                    ), revealing their binding interactions with the active site of AChE, BChE, hCA I and hCA II thus supporting the experimental findings. Additionally,\n                    <jats:italic>in silico<\/jats:italic>\n                    absorption, distribution, metabolism, and excretion (ADME) prediction studies of the obtained compounds (\n                    <jats:bold>2a\u2010<\/jats:bold>\n                    \u2010\n                    <jats:bold>g<\/jats:bold>\n                    ) with\n                    <jats:italic>in silico<\/jats:italic>\n                    approaches were carried out to determine their solubility, whether they have the potential to cross the blood\u2010brain barrier (BBB), values such as GI absorption and drug likeness principles.\n                  <\/jats:p>","DOI":"10.1002\/cbdv.202401849","type":"journal-article","created":{"date-parts":[[2024,8,19]],"date-time":"2024-08-19T13:24:44Z","timestamp":1724073884000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":18,"title":["New Sulfonate Ester\u2010Linked Fluorinated Hydrazone Derivatives as Multitarget Carbonic Anhydrase and Cholinesterase Inhibitors: Design, Synthesis, Biological Evaluation, Molecular Docking and ADME Analysis"],"prefix":"10.1002","volume":"21","author":[{"given":"Berna","family":"Ak\u0131\u015f","sequence":"first","affiliation":[{"name":"Department of Chemistry Graduate Education Institute Batman University  72100 Batman T\u00fcrkiye"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0401-7419","authenticated-orcid":false,"given":"Re\u015fit","family":"\u00c7akmak","sequence":"additional","affiliation":[{"name":"Medical Laboratory Techniques Program Vocational School of Health Services Batman University  72060 Batman T\u00fcrkiye"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Murat","family":"\u015eent\u00fcrk","sequence":"additional","affiliation":[{"name":"Department of Biochemistry Faculty of Pharmacy A\u011fr\u0131 Ibrahim \u00c7ecen University  04100 A\u011fr\u0131 T\u00fcrkiye"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2024,10,18]]},"reference":[{"key":"e_1_2_9_1_1","doi-asserted-by":"publisher","DOI":"10.1021\/cr200176r"},{"key":"e_1_2_9_2_1","doi-asserted-by":"publisher","DOI":"10.1021\/jm501573b"},{"key":"e_1_2_9_3_1","doi-asserted-by":"publisher","DOI":"10.1002\/ardp.202100430"},{"key":"e_1_2_9_4_1","doi-asserted-by":"publisher","DOI":"10.1002\/jmr.2982"},{"key":"e_1_2_9_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.bioorg.2022.106309"},{"key":"e_1_2_9_6_1","doi-asserted-by":"publisher","DOI":"10.1038\/nrd2467"},{"key":"e_1_2_9_7_1","doi-asserted-by":"publisher","DOI":"10.1080\/14756366.2017.1284069"},{"key":"e_1_2_9_8_1","doi-asserted-by":"publisher","DOI":"10.1021\/acs.jmedchem.3c01020"},{"key":"e_1_2_9_9_1","first-page":"125","volume":"38","author":"Sundaram V.","year":"1986","journal-title":"Am. 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