{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,11]],"date-time":"2026-10-11T06:21:02Z","timestamp":1791699662517,"version":"4.3.4"},"reference-count":75,"publisher":"MDPI AG","issue":"22","license":[{"start":{"date-parts":[[2022,11,15]],"date-time":"2022-11-15T00:00:00Z","timestamp":1668470400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"European Regional Development Fund","award":["1.1.1.2\/VIAA\/3\/19\/398"],"award-info":[{"award-number":["1.1.1.2\/VIAA\/3\/19\/398"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>A series of novel 1-(4-benzenesulfonamide)-3-alkyl\/benzyl-hydantoin derivatives were synthesized and evaluated for the inhibition of eukaryotic and human carbonic anhydrases (CAs, EC 4.2.1.1). The prepared compounds were screened for their hCA inhibitory activities against three cytosolic isoforms as well as two \u03b2-CAs from fungal pathogens. The best inhibition was observed against hCA II and VII as well as Candida glabrata enzyme CgNce103. hCA I and Malassezia globosa MgCA enzymes were, on the other hand, less effectively inhibited by these compounds. The inhibitory potency of these compounds against CAs was found to be dependent on the electronic and steric effects of substituent groups on the N3-position of the hydantoin ring, which included alkyl, alkenyl and substituted benzyl moieties. The interesting results against CgNce103 make the compounds of interest for investigations in vivo as potential antifungals.<\/jats:p>","DOI":"10.3390\/ijms232214115","type":"journal-article","created":{"date-parts":[[2022,11,16]],"date-time":"2022-11-16T02:24:53Z","timestamp":1668565493000},"page":"14115","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":20,"title":["Benzenesulfonamides Incorporating Hydantoin Moieties Effectively Inhibit Eukaryoticand Human Carbonic Anhydrases"],"prefix":"10.3390","volume":"23","author":[{"given":"Morteza","family":"Abdoli","sequence":"first","affiliation":[{"name":"Institute of Technology of Organic Chemistry, Faculty of Materials Science and Applied Chemistry, Riga Technical University, P. Valdenaiela 3, LV-1048 Riga, Latvia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Viviana","family":"De Luca","sequence":"additional","affiliation":[{"name":"Department of Biology, Agriculture and Food Sciences, Institute of Biosciences and Bioresources, Via Pietro Castellino 111, 80131 Napoli, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3314-2411","authenticated-orcid":false,"given":"Clemente","family":"Capasso","sequence":"additional","affiliation":[{"name":"Department of Biology, Agriculture and Food Sciences, Institute of Biosciences and Bioresources, Via Pietro Castellino 111, 80131 Napoli, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4262-0323","authenticated-orcid":false,"given":"Claudiu T.","family":"Supuran","sequence":"additional","affiliation":[{"name":"NEUROFARBA Department, Pharmaceutical and Nutraceutical Section, University of Florence, Via Ugo Schiff 6, 50019 Florence, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9471-1342","authenticated-orcid":false,"given":"Raivis","family":"\u017dalubovskis","sequence":"additional","affiliation":[{"name":"Institute of Technology of Organic Chemistry, Faculty of Materials Science and Applied Chemistry, Riga Technical University, P. Valdenaiela 3, LV-1048 Riga, Latvia"},{"name":"Latvian Institute of Organic Synthesis, Aizkraukles 21, LV-1006 Riga, Latvia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2022,11,15]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"967","DOI":"10.1517\/14728222.11.7.967","article-title":"Targeting enzyme inhibitors in drug discovery","volume":"11","author":"Copeland","year":"2007","journal-title":"Expert Opin. Ther. Targets"},{"key":"ref_2","doi-asserted-by":"crossref","unstructured":"Geronikaki, A. (2021). Recent trends in enzyme inhibition and activation in drug design. Molecules, 26.","DOI":"10.3390\/molecules26010017"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1038\/nrd.2017.219","article-title":"Mechanistic enzymology in drug discovery: A fresh perspective","volume":"17","author":"Holdgate","year":"2018","journal-title":"Nat. Rev. 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