Synthesis, characterization, biological activity and molecular docking studies of novel schiff bases derived from thiosemicarbazide: Biochemical and computational approach

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dc.authoridUSANMAZ, HANDE/0000-0003-3851-9601
dc.authoridTaslimi, Parham/0000-0002-3171-0633
dc.authoridMaraman, Muhammet/0000-0002-0155-3390
dc.authoridTOKALI, Feyzi Sinan/0000-0001-5532-8802
dc.contributor.authorTokali, Feyzi Sinan
dc.contributor.authorTaslimi, Parham
dc.contributor.authorUsanmaz, Hande
dc.contributor.authorKaraman, Muhammet
dc.contributor.authorSendil, Kivilcim
dc.date.accessioned2025-03-23T19:39:24Z
dc.date.available2025-03-23T19:39:24Z
dc.date.issued2021
dc.departmentSinop Üniversitesi
dc.description.abstractIn this study, eight new Schiff base derivatives (2a-h) were synthesized and their inhibition activities against Acetylcholinesterase (AChE), Butyrylcholinesterase (BChE), alpha-Glucosidase and Lactoperoxidase (LPO) were investigated. Structures of the synthesized compounds were characterized using H-1 and C-13 nuclear magnetic resonance (NMR), infrared spectroscopy (IR), and high-resolution mass spectrometry (HRMS) spectroscopic methods. AChE was inhibited by these novel Schiff bases (2a-h) in low nanomolar levels, the K-i of which differed between 592.66 +/- 57.04 and 810.78 +/- 84.06 nM. Against BChE, the novel compounds demonstrated Kis varying from 358.31 +/- 37.88 to 577.24 +/- 59.91 nM. Also, these novel Schiff bases effectively inhibited alpha-glucosidase, with K-i values in the range of 1.56 +/- 0.32 to 14.78 +/- 2.57 nM. For LPO, K-i values were in the range of 3.96 +/- 0.37 to 12.75 +/- 0.06 nM. For alpha-glucosidase, the most effective molecules were 2b and 2 g with K-i values of 1.56 +/- 0.32 and 14.78 +/- 2.57 nM, respectively. Molecular docking results showed that the compounds have binding affinity with -5.559,-9.698, -7.606, and -6.971 kcal/mol against LPO, AChE, BChE, and alpha-glucosidase enzyme, respectively. It has been observed that the furan and thiosemicarbazone moieties play an important role in the inhibition of these enzymes. (C) 2020 Elsevier B.V. All rights reserved.
dc.identifier.doi10.1016/j.molstruc.2020.129666
dc.identifier.issn0022-2860
dc.identifier.issn1872-8014
dc.identifier.scopus2-s2.0-85098587429
dc.identifier.scopusqualityQ1
dc.identifier.urihttps://doi.org/10.1016/j.molstruc.2020.129666
dc.identifier.urihttps://hdl.handle.net/11486/6347
dc.identifier.volume1231
dc.identifier.wosWOS:000621281500001
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_20250323
dc.subjectSchiffbases
dc.subjectThiosemicarbazide
dc.subjectCholinesterase
dc.subjectEnzyme inhibition
dc.subjectMolecular docking
dc.titleSynthesis, characterization, biological activity and molecular docking studies of novel schiff bases derived from thiosemicarbazide: Biochemical and computational approach
dc.typeArticle

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