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

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dc.authoridMusatat, Ahmad Badreddin/0000-0002-4137-4901en_US
dc.authoridKerimak-Öner, Mine Nazan/0000-0003-2286-6289en_US
dc.authoridDemirci, Tuna/0000-0001-8933-4944en_US
dc.authorscopusid58985027600en_US
dc.authorscopusid55342808300en_US
dc.authorscopusid57194424657en_US
dc.authorscopusid37099630300en_US
dc.authorscopusid58110944900en_US
dc.authorscopusid57191499641en_US
dc.authorscopusid58984786700en_US
dc.authorwosidGüleç, Özcan/KHX-0521-2024en_US
dc.authorwosidMusatat, Ahmad Badreddin/HHR-8987-2022en_US
dc.authorwosidKerimak-Öner, Mine Nazan/F-7159-2018en_US
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.accessioned2024-08-23T16:04:45Z
dc.date.available2024-08-23T16:04:45Z
dc.date.issued2024en_US
dc.departmentDüzce Üniversitesien_US
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.en_US
dc.description.sponsorshipSiirt University Research Project; [2017-SIUEFEB-83]en_US
dc.description.sponsorshipThis work was supported by the Siirt University Research Project [grant numbers 2017-SIUEFEB-83] .en_US
dc.identifier.doi10.1016/j.ijbiomac.2024.131489
dc.identifier.issn0141-8130
dc.identifier.issn1879-0003
dc.identifier.pmid38608980en_US
dc.identifier.scopus2-s2.0-85190351498en_US
dc.identifier.scopusqualityQ1en_US
dc.identifier.urihttps://doi.org/10.1016/j.ijbiomac.2024.131489
dc.identifier.urihttps://hdl.handle.net/20.500.12684/14346
dc.identifier.volume267en_US
dc.identifier.wosWOS:001230305300001en_US
dc.identifier.wosqualityN/Aen_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.language.isoenen_US
dc.publisherElsevieren_US
dc.relation.ispartofInternational Journal of Biological Macromoleculesen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectBisoxadiazoleen_US
dc.subjectSulfonamideen_US
dc.subjectBovine carbonic anhydrase (bCA)en_US
dc.subjectDFTen_US
dc.subjectMolecular dockingen_US
dc.subjectBasis-Setsen_US
dc.subjectEnzymeen_US
dc.subjectOsteopetrosisen_US
dc.subjectDesignen_US
dc.subjectStateen_US
dc.titleBovine carbonic anhydrase (bCA) inhibitors: Synthesis, molecular docking and theoretical studies of bisoxadiazole-substituted sulfonamide derivativesen_US
dc.typeArticleen_US

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