4-Phenylthiazol-1,2,3-triazole derivatives as new potential α-glucosidase and α-amylase inhibitors

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dc.contributor.authorGhanbarlou, Mehdi
dc.contributor.authorKarimian, Somaye
dc.contributor.authorDoraghi, Fatemeh
dc.contributor.authorDadgar, Armin
dc.contributor.authorSenol, lbilge Merve
dc.contributor.authorLarijani, Bagher
dc.contributor.authorMohammadi-Khanaposhtani, Maryam
dc.date.accessioned2026-04-04T13:34:54Z
dc.date.available2026-04-04T13:34:54Z
dc.date.issued2025
dc.departmentİnönü Üniversitesi
dc.description.abstractType-2 diabetes mellitus (T2DM) can be managed by targeting carbohydrate hydrolases such as alpha-glucosidase and alpha-amylase. In this regard, a new 4-phenylthiazol-benzamide-1,2,3-triazole-N-phenylacetamide scaffold was designed via molecular hybridization (MH), and 15 derivatives (9a-o) were synthesized by changing the substituents on the phenyl ring of the N-phenylacetamide moiety. These compounds were evaluated as potent alpha-glucosidase and alpha-amylase inhibitors. The in vitro results indicated that the half maximal inhibitory concentration (IC50) of compounds 9a-o ranged from 10.71 to 42.35 nM against alpha-glucosidase and 49.17-81.94 nM against alpha-amylase while the IC50 values of the positive control acarbose against alpha-glucosidase and alpha-amylase were 62.03 and 105.44 nM, respectively. The most potent compound against both digestive enzymes was compound 9g with two methyl groups on positions 2 and 3 of the phenyl ring of the N-phenylacetamide moiety. Compound 9g was 5.79 and 2.14 times more potent than acarbose against alpha-glucosidase and alpha-amylase, respectively. The docking study showed that all the synthesized compounds (9a-o) attached to the active sites of alpha-glucosidase and alpha-amylase with lower binding energies in comparison to acarbose. Furthermore, according to the dynamics simulation, compound 9g established a stable complex with the active site of alpha-glucosidase.
dc.identifier.doi10.1016/j.molstruc.2025.141919
dc.identifier.issn0022-2860
dc.identifier.issn1872-8014
dc.identifier.orcid0000-0001-8496-6782
dc.identifier.scopus2-s2.0-85219494968
dc.identifier.scopusqualityQ1
dc.identifier.urihttps://doi.org/10.1016/j.molstruc.2025.141919
dc.identifier.urihttps://hdl.handle.net/11616/109485
dc.identifier.volume1334
dc.identifier.wosWOS:001441752600001
dc.identifier.wosqualityQ2
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.language.isoen
dc.publisherElsevier
dc.relation.ispartofJournal of Molecular Structure
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.snmzKA_WOS_20250329
dc.subjectalpha-Glucosidase
dc.subjectalpha-Amylase
dc.subject4-Phenylthiazol
dc.subjectMolecular docking
dc.subjectDynamics simulations
dc.title4-Phenylthiazol-1,2,3-triazole derivatives as new potential α-glucosidase and α-amylase inhibitors
dc.typeArticle

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