Selenourea and thiourea derivatives of chiral and achiral enetetramines: Synthesis, characterization and enzyme inhibitory properties

dc.contributor.authorYigit, Murat
dc.contributor.authorCelepci, Duygu Barut
dc.contributor.authorTaslimi, Parham
dc.contributor.authorYigit, Beyhan
dc.contributor.authorCetinkaya, Engin
dc.contributor.authorOzdemir, Ismail
dc.contributor.authorAygun, Muhittin
dc.contributor.authorTaslimi, Parham
dc.date.accessioned2025-10-18T10:11:02Z
dc.date.created2022
dc.date.issued2022
dc.departmentFakülteler, Fen Fakültesi, Biyoteknoloji Bölümü
dc.description.abstractA series of chiral and achiral cyclic seleno-and thiourea compounds bearing benzyl groups on N-atoms were prepared from enetetramines and appropriate Group VI elements in good yields. All the synthesized compounds were characterized by elemental analysis, FT-IR, H-1 NMR and C-13 NMR spectroscopy, and the molecular and crystal structures of (R,R)-4b and (R,R)-5b were confirmed by the single-crystal X-ray diffraction method. These assayed for their activities against metabolic enzymes acetylcholinesterase, butyrylcholinesterase, and alpha-glycosidase. These selenourea and thiourea derivatives of chiral and achiral enetetramines effectively inhibit AChE and BChE with IC50 values in the range of 3.32-11.36 and 1.47-9.73 mu M, respectively. Also, these compounds inhibited alpha-glycosidase enzyme with IC50 values varying between 1.37 and 8.53 mu M. The results indicated that all the synthesized compounds exhibited excellent inhibitory activities against mentioned enzymes as compared with standard inhibitors. Representatively, the most potent compound against alpha-glycosidase enzyme, (S,S)-5b, was 12-times more potent than standard inhibitor acarbose; 7b and 8a as most potent compounds against cholinesterase enzymes, were around 5 and 13-times more potent than standard inhibitor tacrine against achethylcholinesterase (AChE) and butyrylcholinesterase (BChE), respectively.
dc.description.sponsorshipDokuz Eylul University [2010.KB.FEN.13]
dc.description.sponsorshipThe authors thank Dokuz Eylul University for the use of the Oxford Rigaku Xcalibur Eos Diffractometer (purchased under University Research Grant No: 2010.KB.FEN.13).
dc.identifier.doi10.1016/j.bioorg.2021.105566
dc.identifier.issn0045-2068
dc.identifier.issn1090-2120
dc.identifier.orcidTaslimi, Parham/0000-0002-3171-0633
dc.identifier.orcidGulcin, ilhami/0000-0001-5993-1668
dc.identifier.orcidAygun, Muhittin/0000-0001-9670-9062
dc.identifier.pmid34974209
dc.identifier.scopus2-s2.0-85121986127
dc.identifier.scopusqualityQ1
dc.identifier.urihttps://doi.org/10.1016/j.bioorg.2021.105566
dc.identifier.urihttps://hdl.handle.net/11772/22170
dc.identifier.volume120
dc.identifier.wosWOS:000788750000012
dc.identifier.wosqualityQ1
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoen
dc.publisherAcademic Press Inc Elsevier Science
dc.relation.ispartofBioorganic Chemistry
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.snmzWoS_20251016
dc.subjectChiral Selenourea
dc.subjectThiourea
dc.subjectEnetetramine
dc.subjectCrystal Structure
dc.subjectEnzyme Inhibition
dc.subjectAchethylcholinesterase
dc.subjectButyrylcholinesterase
dc.titleSelenourea and thiourea derivatives of chiral and achiral enetetramines: Synthesis, characterization and enzyme inhibitory properties
dc.typeArticle
dspace.entity.typePublication
relation.isAuthorOfPublicationdadfa319-65b8-4543-92b4-bea49e0139e9
relation.isAuthorOfPublication.latestForDiscoverydadfa319-65b8-4543-92b4-bea49e0139e9

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