Scopus
🔓 Açık Erişim YÖKSİS DOI Eşleşti
SJR Q3
Synthesis and Molecular Docking of New N-Acyl HydrazonesBenzimidazole as hCA I and II Inhibitors
Medicinal Chemistry · Ocak 2023
YÖKSİS Kayıtları
Synthesis and Molecular Docking of New N-Acyl Hydrazones-Benzimidazole as hCA I and II Inhibitors
Medicinal Chemistry · 2023 SCI-Expanded
Dr. Öğr. Üyesi AYŞEN IŞIK →
Synthesis and Molecular Docking of New N-Acyl Hydrazones-Benzimidazole as hCA I and II Inhibitors
Medicinal Chemistry · 2023 SCI-Expanded
Prof. Dr. KAAN KÜÇÜKOĞLU →
Synthesis and Molecular Docking of New N-Acyl Hydrazones-Benzimidazole as hCA I and II Inhibitors
Medicinal Chemistry · 2023 SCI-Expanded
Dr. Öğr. Üyesi AYŞEN IŞIK →
YÖKSİS Kayıtları — ISSN Eşleşmesi
Synthesis and Molecular Docking of New N-Acyl Hydrazones-Benzimidazole as hCA I and II Inhibitors
2023 ISSN: 1573-4064 SCI-Expanded Q3
Prof. Dr. KAAN KÜÇÜKOĞLU →
Makale Bilgileri
Dergi
Medicinal Chemistry
ISSN15734064
Yayın TarihiOcak 2023
Cilt / Sayfa19 · 485-494
Scopus ID2-s2.0-85153854470
Erişim🔓 Açık Erişim
Özet
Background: The carbonic anhydrases (CAs) which are found in most living organisms is a member of the zinc-containing metalloenzyme family. The abnormal levels and activities are frequently associated with various diseases therefore CAs have become an attractive target for the design of inhibitors or activators that can be used in the treatment of those diseases. Methods: Herein, we have designed and synthesized new benzimidazole-hydrazone derivatives to investigate the effects of these synthesized compounds on CA isoenzymes. Chemical structures of synthesized compounds were confirmed by1H NMR,13C NMR, and HRMS. The synthetic derivatives were screened for their inhibitory potential against carbonic anhydrase I and II by in vitro assay. Results: These compounds have IC50 values of 5.156-1.684 µM (hCA I) and 4.334-2.188 µM (hCA II). Inhibition types and Ki values of the compounds were determined. The Ki values of the compounds were 5.44 ± 0.14 µM-0.299 ± 0.01 µM (hCA I) and 3.699 ± 0.041 µM-1.507 ± 0.01 µM (hCA II). The synthetic compounds displayed inhibitory action comparable to that of the clinically utilized reference substance, acetazolamide. According to this, compound 3p was the most effective molecule with an IC50 value of 1.684 µM. Accordingly, the type of inhibition was noncompetitive and the Ki value was 0.299 ± 0.01 µM. Conclusion: According to the in vitro test results, detailed protein-ligand interactions of the compound 3p, which is more active against hCA I than standard azithromycin (AZM), were analyzed. In addition, the cytotoxic effects of the compounds on the L929 healthy cell line were evaluated.
Yazarlar (8)
1
Kaan Kucukoglu
ORCID: 0000-0001-8977-9775
2
Ulviye Acar Çevik
ORCID: 0000-0003-3537-2544
3
Hayrunnisa Nadaroglu
4
Ismail Celik
ORCID: 0000-0002-8146-1663
5
Ayşen Işık
6
Hayrani Eren Bostancı
7
Yusuf Özkay
8
Zafer Asım Kaplancıklı
Anahtar Kelimeler
benzimidazole
carbonic anhydrase I
carbonic anhydrase II
Hydrazone
molecular docking
MTT
Kurumlar
Anadolu Üniversitesi
Eskisehir Turkey
Atatürk Üniversitesi
Erzurum Turkey
Cumhuriyet Üniversitesi
Sivas Turkey
Erciyes Üniversitesi
Kayseri Turkey
Selçuk Üniversitesi
Selçuklu Turkey
Scimago Dergi (ISSN Eşleşmesi)
Medicinal Chemistry
Q3
SJR Skoru0,417
H-Index54
YayıncıBentham Science Publishers
ÜlkeUnited Arab Emirates
Drug Discovery (Q3)
Metrikler
5
Atıf
8
Yazar
6
Anahtar Kelime