Investigation of the inhibitory effects of human carbonic anhydrase i and jack bean urease by coumarin derivates
MakaleYalnız künye
Özet
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.
Anahtar Kelimeler
RDL Kalıcı Bağlantı (PID)
https://rdlopen.rawdatalibrary.net/r/gumushane/15097Resmi atıflarda kullanılan kalıcı adresTam Kayıt
| Alan | Değer | Dil |
|---|---|---|
| dc.contributor.author | Aygul, Imdat | |
| dc.contributor.author | Karahalil, Fatma Yaylaci | |
| dc.contributor.author | Danis, Ozkan | |
| dc.contributor.author | Ogan, Ayse | |
| dc.contributor.author | Kolayli, Sevgi | |
| dc.date.accessioned | 2026-10-22T10:23:35.143786033Z | |
| dc.date.available | 2026-10-22T10:23:35.143786033Z | |
| dc.date.issued | 2018 | |
| dc.description.abstract | 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. | |
| dc.identifier.doi | 10.2174/1573408014666180903143132 | |
| dc.identifier.endpage | 232 | |
| dc.identifier.issn | 1573-4080 | |
| dc.identifier.issue | 3 | |
| dc.identifier.scopus | 2-s2.0-85062830056 | |
| dc.identifier.startpage | 226 | |
| dc.identifier.uri | https://rdlopen.rawdatalibrary.net/r/gumushane/15097 | |
| dc.identifier.volume | 14 | |
| dc.language.iso | en | |
| dc.publisher | Bentham Science Publishers B.V. | |
| dc.relation.ispartof | Current Enzyme Inhibition | |
| dc.rights | info:eu-repo/semantics/closedAccess | |
| dc.subject | Carbonic anhydrase | |
| dc.subject | Coumarin | |
| dc.subject | Inhibition | |
| dc.subject | Jack bean | |
| dc.subject | Synthesis compounds | |
| dc.subject | Urease | |
| dc.subject.other | 3 (3,4 dihydroxyphenyl) 6,7 dihydroxy 2h chromen 2 one | |
| dc.subject.other | 3 (3,4 dimethoxyphenyl) 5,6,7 trihydroxy 2h chromen 2 one | |
| dc.subject.other | 3 (3,4 dimethoxyphenyl) 6,7 dihydroxy 2h chromen 2 one | |
| dc.subject.other | 4 (3,4 dihydroxyphenyl) 6,7 dihydroxy 2h chromen 2 one | |
| dc.subject.other | 4 (3,4 dimethoxyphenyl) 6,7 dihydroxy 2h chromen 2 one | |
| dc.subject.other | carbonate dehydratase I | |
| dc.subject.other | coumarin derivative | |
| dc.subject.other | unclassified drug | |
| dc.subject.other | urease | |
| dc.subject.other | antimicrobial activity | |
| dc.subject.other | antineoplastic activity | |
| dc.subject.other | antioxidant activity | |
| dc.subject.other | Article | |
| dc.subject.other | DPPH radical scavenging assay | |
| dc.subject.other | drug synthesis | |
| dc.subject.other | enzyme activity | |
| dc.subject.other | enzyme inhibition | |
| dc.subject.other | free radical scavenging assay | |
| dc.subject.other | Helicobacter pylori | |
| dc.subject.other | IC50 | |
| dc.subject.other | ligand binding | |
| dc.subject.other | minimum inhibitory concentration | |
| dc.subject.other | solubility | |
| dc.subject.other | Sporosarcina pasteurii | |
| dc.title | Investigation of the inhibitory effects of human carbonic anhydrase i and jack bean urease by coumarin derivates | |
| dc.type | Article | |
| dspace.entity.type | Publication | |
| rdl.citation.openalex | 1 | |
| rdl.citation.scopus | 2 | |
| rdl.oa.status | closed | |
| rdl.source.index | SCOPUS |
