Synthesis, characterization, and computational study of novel carvacrol-based 2-aminothiol and sulfonic acid derivatives as metabolic enzyme inhibitors

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dc.authoridGenç Bilgiçli, Hayriye/0000-0001-6909-316X
dc.authoridUc, Eda Mehtap/0000-0002-9259-5704
dc.authorwosidGenç Bilgiçli, Hayriye/U-4685-2017
dc.contributor.authorBytyqi-Damoni, Arlinda
dc.contributor.authorUc, Eda Mehtap
dc.contributor.authorBora, Rifat Emin
dc.contributor.authorBilgicli, Hayriye Genc
dc.contributor.authorAlagoz, Mehmet Abdullah
dc.contributor.authorZengin, Mustafa
dc.contributor.authorGulcin, Lhami
dc.date.accessioned2024-08-04T20:55:05Z
dc.date.available2024-08-04T20:55:05Z
dc.date.issued2024
dc.departmentİnönü Üniversitesien_US
dc.description.abstractEight new 2-aminothiols (69-96%) and three new sulfonic acids (51-76%) were synthesized and characterized by NMR and HRMS spectra. This study presents the inhibitory effects of a series of novel carvacrol-based 2-aminothiol and sulfonic acid derivatives (3a-f,4a-c) against human carbonic anhydrase I and II isozymes (hCA I and II) acetylcholinesterase (AChE), butyrylcholinesterase (BChE) and alpha-glycosidase. Ki values were calculated as 12.52 +/- 3.61-335.65 +/- 60.56 nM for hCA I, 12.20 +/- 3.59-389.69 +/- 119.41 nM for hCA II, 1.79 +/- 0.56-84.86 +/- 23.34 nM for AChE, 6.57 +/- 2.54-88.05 +/- 21.05 nM for BChE and 14.63 +/- 4.76-116.39 +/- 33.70 nM alpha-glucosidase enzymes. Also, the inhibition effects of novel carvacrol-based 2-aminothiol (3a -h) and sulfonic acid derivatives (4a -c) were compared to standard and clinically used inhibitors of acetazolamide, Tacrine and acarbose, respectively. Molecular modeling studies of novel compounds, docking scores, and free binding energies were calculated. The activity results of the compounds were found to be compatible with the docking scores. Molecular dynamics studies were conducted with the best activity against CA I and CA II compounds, 4b (IC50: 4.76 nM) and 4a (IC50: 4.36 nM), respectively. In Dynamic Simulation studies, it was observed that the compounds remained stable at the active sites of the proteins.en_US
dc.description.sponsorshipScientific and Technological Research Council of Turkey (TUBITAK) [118Z681]en_US
dc.description.sponsorshipThis study is a part of the project which is supported by Scientific and Technological Research Council of Turkey (TUBITAK Project No: 118Z681) .en_US
dc.identifier.doi10.1016/j.molstruc.2024.137516
dc.identifier.issn0022-2860
dc.identifier.issn1872-8014
dc.identifier.scopus2-s2.0-85185174165en_US
dc.identifier.scopusqualityQ2en_US
dc.identifier.urihttps://doi.org/10.1016/j.molstruc.2024.137516
dc.identifier.urihttps://hdl.handle.net/11616/101820
dc.identifier.volume1303en_US
dc.identifier.wosWOS:001174090100001en_US
dc.identifier.wosqualityN/Aen_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.language.isoenen_US
dc.publisherElsevieren_US
dc.relation.ispartofJournal of Molecular Structureen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectCarvacrolen_US
dc.subjectCarbonic anhydraseen_US
dc.subjectalpha-glucosidaseen_US
dc.subjectAcetylcholinesteraseen_US
dc.subjectButyrylcholinesteraseen_US
dc.titleSynthesis, characterization, and computational study of novel carvacrol-based 2-aminothiol and sulfonic acid derivatives as metabolic enzyme inhibitorsen_US
dc.typeArticleen_US

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