Synthesis, biological activities, and molecular docking studies of triazolo[4,3-b]triazine derivatives as a novel class of ?-glucosidase and ?-amylase inhibitors

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dc.contributor.authorSeyfi, Soheila
dc.contributor.authorSalarinejad, Somayeh
dc.contributor.authorMoghimi, Setareh
dc.contributor.authorToolabi, Mahsa
dc.contributor.authorSadeghian, Nastaran
dc.contributor.authorTuezuen, Burak
dc.contributor.authorFiroozpour, Loghman
dc.date.accessioned2024-10-26T18:11:05Z
dc.date.available2024-10-26T18:11:05Z
dc.date.issued2024
dc.departmentSivas Cumhuriyet Üniversitesi
dc.description.abstractIn diabetes mellitus, amylase and glucosidase enzymes are the primary triggers. The main function of these enzymes is to break macromolecules into simple sugar units, which directly affect blood sugar levels by increasing blood permeability. To overcome this metabolic effect, there is a need for a potent and effective inhibitor capable of suppressing the enzymatic conversion of sugar macromolecules into their smaller units. Herein, we reported the discovery of a series of substituted triazolo[4,3-b][1,2,4]triazine derivatives as alpha-glucosidase and alpha-amylase inhibitors. All target compounds demonstrated significant inhibitory activities against alpha-glucosidase and alpha-amylase enzymes compared with acarbose as the positive control. The most potent compound 10k, 2-[(6-phenyl-[1,2,4]triazolo[4,3-b][1,2,4]triazin-3-yl)thio]-N-[4-(trifluoromethyl)phenyl]acetamide, demonstrated IC50 values of 31.87 and 24.64 nM against alpha-glucosidase and alpha-amylase enzymes, respectively. To study their mechanism of action, kinetic studies were also done, which determined the mode of inhibition of both enzymes. Molecular docking was used to confirm the binding interactions of the most active compounds.
dc.description.sponsorshipNational Institute for Medical Research Development [53816]; National Institute for Medical Research Development (NIMAD) [RGD-020]; Scientific Research Project Fund of Sivas Cumhuriyet University (CUBAP)
dc.description.sponsorshipThis work was supported by a grant from the National Institute for Medical Research Development (NIMAD), grant no. 53816. The numerical calculations reported in this paper were fully/partially performed at TUBITAK ULAKBIM, High Performance and Grid Computing Center (TRUBA resources). This work was supported by the Scientific Research Project Fund of Sivas Cumhuriyet University (CUBAP) under the project number RGD-020.
dc.identifier.doi10.1002/ardp.202300628
dc.identifier.issn0365-6233
dc.identifier.issn1521-4184
dc.identifier.issue7
dc.identifier.pmid38501879
dc.identifier.scopus2-s2.0-85188625206
dc.identifier.scopusqualityQ2
dc.identifier.urihttps://doi.org/10.1002/ardp.202300628
dc.identifier.urihttps://hdl.handle.net/20.500.12418/30500
dc.identifier.volume357
dc.identifier.wosWOS:001187181400001
dc.identifier.wosqualityN/A
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoen
dc.publisherWiley-V C H Verlag Gmbh
dc.relation.ispartofArchiv Der Pharmazie
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectalpha-amylase
dc.subjectalpha-glucosidase
dc.subjectdiabetes
dc.subjectmolecular docking
dc.titleSynthesis, biological activities, and molecular docking studies of triazolo[4,3-b]triazine derivatives as a novel class of ?-glucosidase and ?-amylase inhibitors
dc.typeArticle

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