ADME properties, bioactivity and molecular docking studies of 4-amino-chalcone derivatives: new analogues for the treatment of Alzheimer, glaucoma and epileptic diseases
Yazarlar (6)
Prof. Dr. Mustafa CEYLAN
Tokat Gaziosmanpaşa Üniversitesi, Türkiye
Prof. Dr. Meliha Burcu GÜRDERE
Tokat Gaziosmanpaşa Üniversitesi, Türkiye
Prof. Dr. Yakup BUDAK
Tokat Gaziosmanpaşa Üniversitesi, Türkiye
Sivas Cumhuriyet Üniversitesi, Türkiye
Türkiye
Türkiye
| Makale Türü |
Özgün Makale
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| Makale Alt Türü | Diğer hakemli uluslarası dergilerde yayınlanan tam makale |
| Dergi Adı | In Silico Pharmacology |
| Dergi ISSN | 2193-9616 |
| Dergi Tarandığı Indeksler | EBSCO |
| Makale Dili | İngilizce |
| Basım Tarihi | 01-2021 |
| Cilt No | 9 |
| Sayı | 34 |
| DOI Numarası | 10.1007/s40203-021-00094-x |
| Makale Linki | http://dx.doi.org/10.1007/s40203-021-00094-x |
| Özet |
| In this study, in vitro inhibition effects of (E)-1-(4-aminophenyl)-3-(aryl) prop-2-en-1-one (4-amino-chalcones) derivatives (3a–o) on acetylcholinesterase (AChE) enzyme and human erythrocyte carbonic anhydrase I and II isoenzymes (hCA I- II) were investigated. And also, the biological activities of 4-amino-chalcone derivatives against enzymes which names are acetylcholinesterase (PDB ID: 1OCE), human Carbonic Anhydrase I (PDB ID: 2CAB), human carbonic anhydrase II (PDB ID: 3DC3), were compared. After the results obtained, ADME/T analysis was performed in order to use 4-amino-chalcone derivatives as a drug in the future. Effective inhibitors of carbonic anhydrase I and II isozymes (hCAI and II) and acetylcholinesterase (AChE) enzymes with Ki values in the range of 2.55 ± 0.35–11.75 ± 3.57 nM for hCA I, 4.31 ± 0.78–17.55 ± 5.86 nM for hCA II and 96.01 ± 25.34–1411.41 ± 32.88 nM for … |
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BM Sürdürülebilir Kalkınma Amaçları
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| Google Scholar | 22 |