Design, synthesis, and inhibition of ?-glucosidase by novel L-phenylalanine-derived hydrazones: Kinetic, molecular docking, and dynamics studies

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dc.authorid0000-0002-1330-6194
dc.contributor.authorKalay, Erbay
dc.contributor.authorAdem, Sevki
dc.contributor.authorDemir, Yeliz
dc.contributor.authorAslan, Osman Nuri
dc.contributor.authorSahin, Engin
dc.contributor.authorEyupoglu, Volkan
dc.contributor.authorComakli, Veysel
dc.date.accessioned2026-02-28T12:17:46Z
dc.date.available2026-02-28T12:17:46Z
dc.date.issued2025
dc.departmentBayburt Üniversitesi
dc.description.abstractIn this paper, a series of novel hydrazones derived from L-phenyl alanine were synthesized in four steps and employed to inhibit alpha-glucosidase through kinetic studies, molecular docking, and molecular dynamics analyses. Among the synthesized compounds, 8, 15, and 16 exhibited the strongest inhibitory effects, with IC50 values of 31.08 mu M, 24.15 mu M, and 19.47 mu M, respectively, surpassing the standard inhibitor acarbose (79.63 mu M). Molecular docking studies revealed robust interactions, with compound 16 achieving the highest MolDock score of -176.316. Molecular dynamics simulations were conducted to evaluate the binding affinity of compound 16 to the isomaltase enzyme from Saccharomyces cerevisiae (3A4A). The most favorable docking pose was subjected to further analysis through MD simulations under dynamic conditions. The MMGBSA analysis of the simulation cluster indicated a strong binding affinity of approximately -43.06 kcal/mol, highlighting the compound's potential for modulating alpha-glucosidase activity. These results underscore the potential of bromine and hydroxylsubstituted hydrazones to modulate isomaltase activity, with therapeutic implications for hyperglycemia and obesity management.
dc.identifier.doi10.1016/j.abb.2025.110368
dc.identifier.issn0003-9861
dc.identifier.issn1096-0384
dc.identifier.pmid40049269
dc.identifier.scopus2-s2.0-86000173226
dc.identifier.scopusqualityQ1
dc.identifier.urihttps://doi.org/10.1016/j.abb.2025.110368
dc.identifier.urihttps://hdl.handle.net/20.500.12403/5970
dc.identifier.volume768
dc.identifier.wosWOS:001444082500001
dc.identifier.wosqualityQ2
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoen
dc.publisherElsevier Science Inc
dc.relation.ispartofArchives of Biochemistry And Biophysics
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.snmzKA_WoS_20260218
dc.subjectHydrazones
dc.subjectMolecular docking
dc.subjectAnd molecular dynamics
dc.subjectalpha-Glucosidase
dc.titleDesign, synthesis, and inhibition of ?-glucosidase by novel L-phenylalanine-derived hydrazones: Kinetic, molecular docking, and dynamics studies
dc.typeArticle

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