Investigation of the inhibitory effects of human carbonic anhydrase i and jack bean urease by coumarin derivates

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Introduction: This study investigated the in vitro inhibition properties of newly synthesized coumarin derivates (C1-C5) against human carbonic anhdyrase I (hCA-I) and jack bean urease. Activities were expressed as IC50 (mg/mL), the concentration reducing 50% of the enzymes. The IC50 values for hCA-I ranged 5.20 µM from 12.10 µM, with compound C3 exhibiting the highest activity. The inhibition values for urease ranged 22.30 µM to 39.00 µM, the highest activity being observed in C5. Conclusion: Comparing the inhibitions with standard inhibitors of the enzymes, while the samples exhibited moderate inhibitions against hCA I, high inhibition was determined against urease.

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AlanDeğerDil
dc.contributor.authorAygul, Imdat
dc.contributor.authorKarahalil, Fatma Yaylaci
dc.contributor.authorDanis, Ozkan
dc.contributor.authorOgan, Ayse
dc.contributor.authorKolayli, Sevgi
dc.date.accessioned2026-10-22T10:23:35.143786033Z
dc.date.available2026-10-22T10:23:35.143786033Z
dc.date.issued2018
dc.description.abstractIntroduction: This study investigated the in vitro inhibition properties of newly synthesized coumarin derivates (C1-C5) against human carbonic anhdyrase I (hCA-I) and jack bean urease. Activities were expressed as IC50 (mg/mL), the concentration reducing 50% of the enzymes. The IC50 values for hCA-I ranged 5.20 µM from 12.10 µM, with compound C3 exhibiting the highest activity. The inhibition values for urease ranged 22.30 µM to 39.00 µM, the highest activity being observed in C5. Conclusion: Comparing the inhibitions with standard inhibitors of the enzymes, while the samples exhibited moderate inhibitions against hCA I, high inhibition was determined against urease.
dc.identifier.doi10.2174/1573408014666180903143132
dc.identifier.endpage232
dc.identifier.issn1573-4080
dc.identifier.issue3
dc.identifier.scopus2-s2.0-85062830056
dc.identifier.startpage226
dc.identifier.urihttps://rdlopen.rawdatalibrary.net/r/gumushane/15097
dc.identifier.volume14
dc.language.isoen
dc.publisherBentham Science Publishers B.V.
dc.relation.ispartofCurrent Enzyme Inhibition
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectCarbonic anhydrase
dc.subjectCoumarin
dc.subjectInhibition
dc.subjectJack bean
dc.subjectSynthesis compounds
dc.subjectUrease
dc.subject.other3 (3,4 dihydroxyphenyl) 6,7 dihydroxy 2h chromen 2 one
dc.subject.other3 (3,4 dimethoxyphenyl) 5,6,7 trihydroxy 2h chromen 2 one
dc.subject.other3 (3,4 dimethoxyphenyl) 6,7 dihydroxy 2h chromen 2 one
dc.subject.other4 (3,4 dihydroxyphenyl) 6,7 dihydroxy 2h chromen 2 one
dc.subject.other4 (3,4 dimethoxyphenyl) 6,7 dihydroxy 2h chromen 2 one
dc.subject.othercarbonate dehydratase I
dc.subject.othercoumarin derivative
dc.subject.otherunclassified drug
dc.subject.otherurease
dc.subject.otherantimicrobial activity
dc.subject.otherantineoplastic activity
dc.subject.otherantioxidant activity
dc.subject.otherArticle
dc.subject.otherDPPH radical scavenging assay
dc.subject.otherdrug synthesis
dc.subject.otherenzyme activity
dc.subject.otherenzyme inhibition
dc.subject.otherfree radical scavenging assay
dc.subject.otherHelicobacter pylori
dc.subject.otherIC50
dc.subject.otherligand binding
dc.subject.otherminimum inhibitory concentration
dc.subject.othersolubility
dc.subject.otherSporosarcina pasteurii
dc.titleInvestigation of the inhibitory effects of human carbonic anhydrase i and jack bean urease by coumarin derivates
dc.typeArticle
dspace.entity.typePublication
rdl.citation.openalex1
rdl.citation.scopus2
rdl.oa.statusclosed
rdl.source.indexSCOPUS