Scopus
YÖKSİS Eşleşti
Design, synthesis, and molecular docking studies of benzimidazole-1,3,4-triazole hybrids as carbonic anhydrase I and II inhibitors
Chemical Biology and Drug Design · Ocak 2024
YÖKSİS Kayıtları
Design, synthesis, and molecular docking studies of benzimidazole- 1,3,4- triazole hybrids as carbonic anhydrase I and II inhibitors
Chemical Biology & Drug Design · 2024 SCI-Expanded
DOKTOR ÖĞRETİM ÜYESİ AYŞEN IŞIK →
Design, synthesis, and molecular docking studies of benzimidazole- 1,3,4- triazole hybrids as carbonic anhydrase I and II inhibitors
Chemical Biology & Drug Design · 2023 SCI-Expanded
DOKTOR ÖĞRETİM ÜYESİ AYŞEN IŞIK →
Design, synthesis, and molecular docking studies of benzimidazole-1,3,4-triazole hybrids as carbonic anhydrase I and II inhibitors
Chemical Biology & Drug Design · 2024 SCI-Expanded
PROFESÖR KAAN KÜÇÜKOĞLU →
Makale Bilgileri
DergiChemical Biology and Drug Design
Yayın TarihiOcak 2024
Cilt / Sayfa103
Scopus ID2-s2.0-85170707517
Özet
In this study, with an aim to develop novel heterocyclic hybrids as potent enzyme inhibitors, we synthesized a series of 10 novel 2-(4-(4-ethyl-5-(2-(substitutedphenyl)-2-oxo-ethylthio)-4H-1,2,4-triazol-3-yl)-phenyl)-5,6-dimethyl-1H-benzimidazole (5a–5j) derivatives and characterized by 1H-NMR, 13C-NMR, and HRMS. These compounds were evaluated for their inhibitory activity against hCA I and hCA II. All the compounds exhibited good hCA I and hCA II inhibitory activities with IC50 values in range of 1.288 μM–3.122 μM. Among all these compounds, compound 5e, with an IC50 value of 1.288 μM is the most active against carbonic hCA I. Compound 5h with an IC50 value of 1.532 μM is the most active against carbonic hCA-II. Compounds 5a–5j were also evaluated for their cytotoxic effects on the L929 mouse fibroblast (normal) cell line. The compounds were also analyzed for their antioxidant capacity by TAS, FRAP, and DPPH activity. Enzyme inhibition kinetics showed all compounds 5a–5j to inhibit the enzyme by non-competitive. The most active compound 5e for hCA I and compound 5h for hCA-II were subjected to molecular docking, which revealed their binding interactions with the enzyme's active site, confirming the experimental findings.
Yazarlar (8)
1
Ismail Celik
ORCID: 0000-0002-8146-1663
2
Ulviye Acar Çevik
ORCID: 0000-0003-3537-2544
3
Kaan Kucukoglu
ORCID: 0000-0001-8977-9775
4
Hayrunnisa Nadaroglu
5
Hayrani Eren Bostancı
6
Ayşen Işık
7
Yusuf Özkay
8
Zafer Asım Kaplancıklı
Anahtar Kelimeler
1,3,4-triazole
antioxidant
benzimidazole
carbonic anhydrase
molecular docking
Kurumlar
Anadolu Üniversitesi
Eskisehir Turkey
Atatürk Üniversitesi
Erzurum Turkey
Cumhuriyet Üniversitesi
Sivas Turkey
Erciyes Üniversitesi
Kayseri Turkey
Selçuk Üniversitesi
Selçuklu Turkey
Metrikler
1
Atıf
8
Yazar
5
Anahtar Kelime