Bovine carbonic anhydrase (bCA) inhibitors: Synthesis, molecular docking and theoretical studies of bisoxadiazole-substituted sulfonamide derivatives

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dc.authoridARSLAN, Mustafa/0000-0003-0796-4374
dc.authoridKerimak-Oner, Mine Nazan/0000-0003-2286-6289
dc.authoridMUSATAT, AHMAD BADREDDIN/0000-0002-4137-4901
dc.authoridDemirci, Tuna/0000-0001-8933-4944
dc.contributor.authorEybek, Abdulbaki
dc.contributor.authorKaya, Mustafa Oguzhan
dc.contributor.authorGulec, Ozcan
dc.contributor.authorDemirci, Tuna
dc.contributor.authorMusatat, Ahmad Badreddin
dc.contributor.authorOzdemir, Oguzhan
dc.contributor.authorOner, Mine Nazan Kerimak
dc.date.accessioned2024-12-24T19:27:13Z
dc.date.available2024-12-24T19:27:13Z
dc.date.issued2024
dc.departmentSiirt Üniversitesi
dc.description.abstractThis paper describes the in vitro inhibition potential of bisoxadiazole-substituted sulfonamide derivatives (6a-t) against bovine carbonic anhydrase (bCA) after they were designed through computational analyses and evaluated the predicted interaction via molecular docking. First, in silico ADMET predictions and physicochemical property analysis of the compounds provided insights into solubility and permeability, then density functional theory (DFT) calculations were performed to analyse their ionization energies, nucleophilicity, in vitro electron affinity, dipole moments and molecular interactions under vacuum and dimethyl sulfoxide (DMSO) conditions. After calculating the theoretical inhibition constants, IC50 values determined from enzymatic inhibition were found between 12.93 and 45.77 mu M. Molecular docking evaluation revealed favorable hydrogen bonding and pi-interactions of the compounds within the bCA active site. The experimentally most active compound, 6p, exhibited the strongest inhibitory activity with a theoretical inhibition constant value of 9.41 nM and H-bonds with Gln91, Thr198, and Trp4 residues and His63 Pi-cation interactions with His63 residues. Overall, the study reveals promising bCA blocking potential for the synthesized derivatives, similar to acetazolamide.
dc.description.sponsorshipSiirt University Research Project; [2017-SIUEFEB-83]
dc.description.sponsorshipThis work was supported by the Siirt University Research Project [grant numbers 2017-SIUEFEB-83] .
dc.identifier.doi10.1016/j.ijbiomac.2024.131489
dc.identifier.issn0141-8130
dc.identifier.issn1879-0003
dc.identifier.pmid38608980
dc.identifier.scopus2-s2.0-85190351498
dc.identifier.scopusqualityQ1
dc.identifier.urihttps://doi.org/10.1016/j.ijbiomac.2024.131489
dc.identifier.urihttps://hdl.handle.net/20.500.12604/6536
dc.identifier.volume267
dc.identifier.wosWOS:001230305300001
dc.identifier.wosqualityN/A
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoen
dc.publisherElsevier
dc.relation.ispartofInternational Journal of Biological Macromolecules
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.snmzKA_20241222
dc.subjectBisoxadiazole
dc.subjectSulfonamide
dc.subjectBovine carbonic anhydrase (bCA)
dc.subjectDFT
dc.subjectMolecular docking
dc.titleBovine carbonic anhydrase (bCA) inhibitors: Synthesis, molecular docking and theoretical studies of bisoxadiazole-substituted sulfonamide derivatives
dc.typeArticle

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