Substituted bisbenzimidazole derivatives as multiple targeting agents to treat Alzheimer's disease, diabetes, and microbial infections

Basit Öğe Kaydı
dc.contributor.authorAlgul, Oztekin
dc.contributor.authorMete, Burak
dc.contributor.authorTurkmenoglu, Burcin
dc.contributor.authorSaglamtas, Ruya
dc.contributor.authorAlagoz, M. Abdullah
dc.contributor.authorDogen, Aylin
dc.contributor.authorGulcin, Ilhami
dc.date.accessioned2026-04-04T13:34:54Z
dc.date.available2026-04-04T13:34:54Z
dc.date.issued2025
dc.departmentİnönü Üniversitesi
dc.description.abstractThis study presents the synthesis and bioactivity screening of a series of substituted bisbenzimidazoles (3a-l), assessed for their inhibitory effects on alpha-glycosidase, alpha-amylase, acetylcholinesterase (AChE), butyrylcholinesterase (BChE), as well as their antibacterial activities and metal chelation properties. Compound 3e exhibited the most significant inhibitory activity against intestinal alpha-glycosidase and alpha-amylase, showing IC50 values of 15.51 mu M and 18.18 mu M, respectively. All bisbenzimidazole derivatives demonstrated significant inhibitory activities, with Ki values between 0.99 and 2.98 nM for AChE and 0.40 to 2.18 nM for BChE. Antimicrobial analyses revealed significant antibacterial efficacy in compounds 3c and 3f, with IC50 values ranging from 10.75 to 12.83 mu g/mu L. This article presents a thorough evaluation of the pharmacological activities associated with bisbenzimidazole compounds 3a-l. To validate experimental results, selected compounds exhibiting notable enzyme inhibitory potential were subjected to molecular docking studies, which demonstrated their binding interactions within the active sites of target enzymes. Molecular dynamics simulation studies were carried out for 100 ns to determine the stability of the compounds in target proteins. During the simulation, it was observed that 3 h, 3 g, 3l, and 3e were stable in 4EY7, 4BDS, 3TOP, and 2QV4, respectively. Compounds 3 h, 3 g, 3e, and 3l have been identified as promising candidates for the inhibition of AChE, BChE, alpha-glycosidase, and alpha-amylase, respectively.
dc.description.sponsorshipMersin University [BAP-SBE-2017-2-TP2-2510]
dc.description.sponsorshipWe thank Mersin University for their financial support (BAP-SBE-2017-2-TP2-2510) . The authors would also like to thank Mersin University Advanced Technology Education, Research and Application Center (MEITAM) for their valuable assistance and Erzincan Binali Y & imath;ld & imath;r & imath;m University, Basic Sciences Application and Research Center (EBYU-EUTAM) for the Schrodinger Maestro 2021-2 program
dc.identifier.doi10.1016/j.molstruc.2024.140800
dc.identifier.issn0022-2860
dc.identifier.issn1872-8014
dc.identifier.orcid0000-0002-5770-0847
dc.identifier.orcid0000-0002-4400-2302
dc.identifier.scopus2-s2.0-85209663506
dc.identifier.scopusqualityQ1
dc.identifier.urihttps://doi.org/10.1016/j.molstruc.2024.140800
dc.identifier.urihttps://hdl.handle.net/11616/109488
dc.identifier.volume1323
dc.identifier.wosWOS:001363580800001
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.subjectBisbenzimidazole
dc.subjectEnzyme inhibition
dc.subjectAntimicrobial activity
dc.subjectStructure-activity relationship
dc.subjectMolecular docking
dc.titleSubstituted bisbenzimidazole derivatives as multiple targeting agents to treat Alzheimer's disease, diabetes, and microbial infections
dc.typeArticle

Dosyalar

Koleksiyon

WoS İndeksli Yayınlar Koleksiyonu
Scopus İndeksli Yayınlar Koleksiyonu