Bisbenzimidazole salts and their in silico-in vitro inhibitory abilities on hCA I, hCA II, and AChE enzymes

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dc.authoridAktaş, Aydın/0000-0001-8496-6782
dc.authoridDemir, Yeliz/0000-0003-3216-1098
dc.authoridYilmaz, Ulku/0000-0002-2806-4781
dc.authorwosidAktaş, Aydın/J-6194-2019
dc.authorwosidDemir, Yeliz/ABI-5719-2020
dc.authorwosidYilmaz, Ulku/AAA-7545-2020
dc.contributor.authorYilmaz, Ulku
dc.contributor.authorDemir, Yeliz
dc.contributor.authorTok, Tugba Taskin
dc.contributor.authorGok, Yetkin
dc.contributor.authorAktas, Aydin
dc.contributor.authorGulcin, Ilhami
dc.date.accessioned2024-08-04T20:55:58Z
dc.date.available2024-08-04T20:55:58Z
dc.date.issued2024
dc.departmentİnönü Üniversitesien_US
dc.description.abstractEight new bisbenzimidazolium halides were prepared from alkyl halides and 4,4 '-bis[(benzimidazol-1-yl)methyl]-1,1 '-biphenyl.The structures of the benzimidazole salts were characterized using elemental analysis techniques as well as 1H, 13C NMR, and FT-IR spectroscopic methods. The inhibitory effects of the benzimidazole derivatives were measured against human carbonic anhydrase I (hCA I), human carbonic anhydrase II (hCA II), and acetylcholinesterase (AChE) enzymes. All benzimidazolium halides exhibited significant enzyme inhibitory properties. They showed highly potent inhibitory effect on AChE and hCAs (Ki values are in the range of 15.7 +/- 0.8 to 49.7 +/- 10.1 nM, 14.6 +/- 1.5 to 70.7 +/- 2.7 nM, and 17.4 +/- 2.8 to 38 +/- 10 nM for AChE, hCA I, and hCA II, respectively). The binding orientation of the synthesized bisbenzimidazolium halides was evaluated by molecular docking studies, reflecting the importance of the p-methylbenzyl, m-methylbenzyl, p-nitrophenethyl, and 3-(1,3-dioxoisoindolin-2-yl)methyl) groups in protein-ligand interaction. The docking results support the Ki values of the respective compounds in this study. The structure-activity relationships against the various targets are clearly shown in three dimensions at the atomic level by their interactions with the mentioned enzymes.en_US
dc.identifier.doi10.1007/s00706-024-03204-5
dc.identifier.endpage662en_US
dc.identifier.issn0026-9247
dc.identifier.issn1434-4475
dc.identifier.issue6en_US
dc.identifier.scopus2-s2.0-85192507806en_US
dc.identifier.scopusqualityQ3en_US
dc.identifier.startpage653en_US
dc.identifier.urihttps://doi.org/10.1007/s00706-024-03204-5
dc.identifier.urihttps://hdl.handle.net/11616/101977
dc.identifier.volume155en_US
dc.identifier.wosWOS:001220844700002en_US
dc.identifier.wosqualityN/Aen_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.language.isoenen_US
dc.publisherSpringer Wienen_US
dc.relation.ispartofMonatshefte Fur Chemieen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectBisbenzimidazole salten_US
dc.subjecthCA Ien_US
dc.subjecthCA IIen_US
dc.subjectAChEen_US
dc.subjectIn silicoen_US
dc.subjectIn vitroen_US
dc.titleBisbenzimidazole salts and their in silico-in vitro inhibitory abilities on hCA I, hCA II, and AChE enzymesen_US
dc.typeArticleen_US

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