New 1E,1′E-hydrazine-bis(phenoxy-1,2,3-triazol-acetamide) derivatives as potent inhibitors against acetylcholinesterase, butyrylcholinesterase, and α-glucosidase

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dc.contributor.authorKermaninia, Shahab
dc.contributor.authorMohammadi-Khanaposhtani, Maryam
dc.contributor.authorSenol, Halil
dc.contributor.authorKhajeh Mohammadilar, Fatemeh Sadat
dc.contributor.authorDastyafteh, Navid
dc.contributor.authorMoradkhani, Fatemeh
dc.contributor.authorSaeedi, Saeedeh
dc.date.accessioned2026-04-04T13:34:40Z
dc.date.available2026-04-04T13:34:40Z
dc.date.issued2025
dc.departmentİnönü Üniversitesi
dc.description.abstractIn this study, novel 1E,1 ' E-hydrazine-bis(phenoxy-1,2,3-triazol-acetamide) derivatives 10a-n were synthesized, and because of their structural features, they were evaluated against acetylcholinesterase (AChE), butyrylcholinesterase (BChE), and alpha-glucosidase. AChE and BChE are two important targets in the treatment of Alzheimer's disease (AD), and alpha-glucosidase is a carbohydrate-hydrolyzing enzyme with therapeutic importance in diabetes. Furthermore, cell studies were performed on the title compounds against SH-SY5Y neuroblastoma cells as a cancer cell line and HEK293 cells as a normal cell line. In vitro enzymatic evaluations demonstrated that these new compounds were active against the studied enzymes in comparison to standard inhibitors. In this regard, all the synthesized compounds were more potent than the standard inhibitors tacrine and donepezil against BChE, and most of these compounds were more potent than tacrine against AChE. Moreover, most of the target synthesized compounds were more potent than the standard inhibitor acarbose against alpha-glucosidase. The most potent compound against AChE and BChE was the 2,4-dichloro derivative 10k, and the most potent compound against alpha-glucosidase was the 2-chloro derivative 10h. Moreover, in vitro cell studies demonstrated that compounds 10k and 10h with a selectivity index of >10 demonstrated more cytotoxic effects on the cancer cell line SH-SY5Y than on the normal cell line HEK293. A docking study showed that the latter compounds attached to the active sites of the target enzymes with binding energies more favorable than those of the selected standard inhibitors. Furthermore, docking studies demonstrated that compound 10k interacted with both the catalytic and peripheral anionic sites of AChE and BChE. This property led to the better efficacy of the compound in the treatment of AD.
dc.identifier.doi10.1039/d5ra03877d
dc.identifier.endpage29971
dc.identifier.issn2046-2069
dc.identifier.issue36
dc.identifier.orcid0000-0002-8333-035X
dc.identifier.orcid0000-0001-7664-9664
dc.identifier.pmid40860056
dc.identifier.scopus2-s2.0-105013844514
dc.identifier.scopusqualityQ1
dc.identifier.startpage29960
dc.identifier.urihttps://doi.org/10.1039/d5ra03877d
dc.identifier.urihttps://hdl.handle.net/11616/109310
dc.identifier.volume15
dc.identifier.wosWOS:001555796700001
dc.identifier.wosqualityQ2
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoen
dc.publisherRoyal Soc Chemistry
dc.relation.ispartofRsc Advances
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/openAccess
dc.snmzKA_WOS_20250329
dc.titleNew 1E,1′E-hydrazine-bis(phenoxy-1,2,3-triazol-acetamide) derivatives as potent inhibitors against acetylcholinesterase, butyrylcholinesterase, and α-glucosidase
dc.typeArticle

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