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Influence of chirality of benzimidazole amine hybrids on inhibition of human erythrocytes carbonic anhydrase I, II and acetylcholinesterase

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dc.contributor.authorABDURRAHMANOĞLU, SUZAN
dc.contributor.authorsTunç T., ABDURRAHMANOĞLU S., Günel A., Alım Z., Demirel N.
dc.date.accessioned2023-06-12T10:31:44Z
dc.date.available2023-06-12T10:31:44Z
dc.date.issued2023-01-01
dc.description.abstractNovel chiral benzimidazole amine hybrids (4a–4d) were synthesized from commercially available amine [(R)- (+)-phenylethylamine, (−) (S)-(-)-phenylethylamine, (−) (R)-(-)-cyclohexylethylamine, (S)-(+)-cyclohexylethylamine] and 2-(chloromethyl)-N-tosyl-1H-benzimidazole. The synthesized compounds (4a–4d) were characterized by IR, NMR, and LC/MS analysis. The inhibitory effect of 4a–4d on human erythrocytes carbonic anhydrase I (hCA-I), II (hCA-II), and acetylcholinesterase (AChE) activity was investigated. For hCA-I, the IC50 values of 4a–4d were found to be 4.895 μM, 1.750 μM, 0.173 μM, and 0.620 μM, respectively, and for hCA-II, the IC50 values of 4a–4d were found to be 0.469 μM, 0.380 μM, 0.233 μM, 0.635 μM, respectively. Furthermore, IC50 values of 4a–4d on AChE were found as 87.5 nM, 100 nM, 26.92 nM, and 100 nM, respectively. In addition, molecular docking analysis was performed to evaluate the affinity of 4a–4d against hCA-I, hCA-II, and AChE and explain their binding interactions.
dc.identifier.citationTunç T., ABDURRAHMANOĞLU S., Günel A., Alım Z., Demirel N., "Influence of Chirality of Benzimidazole Amine Hybrids on Inhibition of Human Erythrocytes Carbonic Anhydrase I, II and Acetylcholinesterase", Chemistry and Biodiversity, 2023
dc.identifier.doi10.1002/cbdv.202300207
dc.identifier.issn1612-1872
dc.identifier.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85160637183&origin=inward
dc.identifier.urihttps://hdl.handle.net/11424/290195
dc.language.isoeng
dc.relation.ispartofChemistry and Biodiversity
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectBiyomedikal Mühendisliği
dc.subjectYaşam Bilimleri
dc.subjectBiyoteknoloji
dc.subjectMoleküler Biyoloji ve Genetik
dc.subjectSitogenetik
dc.subjectKimya
dc.subjectTemel Bilimler
dc.subjectMühendislik ve Teknoloji
dc.subjectBiomedical Engineering
dc.subjectLife Sciences
dc.subjectBiotechnology
dc.subjectMolecular Biology and Genetics
dc.subjectCytogenetic
dc.subjectChemistry
dc.subjectNatural Sciences
dc.subjectEngineering and Technology
dc.subjectMühendislik, Bilişim ve Teknoloji (ENG)
dc.subjectTemel Bilimler (SCI)
dc.subjectYaşam Bilimleri (LIFE)
dc.subjectMühendislik
dc.subjectMikrobiyoloji
dc.subjectBİYOKİMYA VE MOLEKÜLER BİYOLOJİ
dc.subjectBİYOTEKNOLOJİ VE UYGULAMALI MİKROBİYOLOJİ
dc.subjectMÜHENDİSLİK, BİYOMEDİKAL
dc.subjectEngineering, Computing & Technology (ENG)
dc.subjectNatural Sciences (SCI)
dc.subjectLife Sciences (LIFE)
dc.subjectENGINEERING
dc.subjectCHEMISTRY
dc.subjectMOLECULAR BIOLOGY & GENETICS
dc.subjectMICROBIOLOGY
dc.subjectBIOCHEMISTRY & MOLECULAR BIOLOGY
dc.subjectBIOTECHNOLOGY & APPLIED MICROBIOLOGY
dc.subjectENGINEERING, BIOMEDICAL
dc.subjectBiyomühendislik
dc.subjectFizik Bilimleri
dc.subjectBiyokimya
dc.subjectGenel Kimya
dc.subjectMoleküler Tıp
dc.subjectMoleküler Biyoloji
dc.subjectBioengineering
dc.subjectPhysical Sciences
dc.subjectBiochemistry
dc.subjectGeneral Chemistry
dc.subjectMolecular Medicine
dc.subjectMolecular Biology
dc.subjectacetylcholinesterase
dc.subjectcarbonic anhydrase
dc.subjectchiral benzimidazole
dc.subjectinhibition
dc.subjectmolecular docking
dc.titleInfluence of chirality of benzimidazole amine hybrids on inhibition of human erythrocytes carbonic anhydrase I, II and acetylcholinesterase
dc.typearticle
dspace.entity.typePublication
local.avesis.ide0092e87-df8e-4af4-b47a-bd7c9ebe0767
local.indexed.atPUBMED
local.indexed.atSCOPUS
relation.isAuthorOfPublicationc4f5249d-7638-47df-be54-950af42ffa85
relation.isAuthorOfPublication.latestForDiscoveryc4f5249d-7638-47df-be54-950af42ffa85

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