Synthesis of benzimidazole derivatives containing amide bond and biological evaluation as acetylcholinesterase, carbonic anhydrase I and II inhibitors

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Atıf İçin Kopyala

Alim Z., Tunc T., Demirel N., Guenel A., KARACAN N.

JOURNAL OF MOLECULAR STRUCTURE, cilt.1268, 2022 (SCI-Expanded)

• Yayın Türü: Makale / Tam Makale
• Cilt numarası: 1268
• Basım Tarihi: 2022
• Doi Numarası: 10.1016/j.molstruc.2022.133647
• Dergi Adı: JOURNAL OF MOLECULAR STRUCTURE
• Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, Chemical Abstracts Core, INSPEC
• Anahtar Kelimeler: Acetylcholinesterase, Benzimidazole, Carbonic anhydrase, Inhibition, Molecular docking, CHIRAL BENZIMIDAZOLES, POTENT ANTIBACTERIAL, ESTERASE-ACTIVITIES, BINDING, DESIGN, IDENTIFICATION, NUCLEOSIDES, ANTIFUNGAL, BIOFILM, SERIES
• Gazi Üniversitesi Adresli: Evet

Özet

Acetylcholinesterase (AChE) and carbonic anhydrase I (CA-I) and II (CA-II) are two vital metabolic enzymes. AChE inhibitors are seen as target molecules in drug development studies for Alzheimer's treatment. CA inhibitors are target molecules for treating many diseases from glaucoma to cancer. For this reason, it is crucial to identify new AChE and CA inhibitors. In this study, four benzimidazole acetamide derivatives were synthesized and their inhibition effects were investigated against human erythrocyte carbonic anhydrase I (hCA-I), II (hCA-II), and AChE. IC50 values of 9a-10b were determined in the range of 0.936 to 17.07 mu M for AChE. IC50 values of 9a-10b for hCA-I were found as 7.21 mu M, 4.72 mu M, 6.08 mu M, 8.23 mu M, respectively. On the other hand, IC50 values of 9a-9b for hCA-II were found as 8.64 mu M, 7.07 mu M, 4.12 mu M, 5.93 mu M, respectively. According to IC50 values, 9a -10b molecules exhibited strong inhibition effects for AChE and hCAI, II. Also, Molecular docking studies were carried out to explain the binding interaction of 9a -10b with AChE, hCA-I, and hCA-II. (C) 2022 Elsevier B.V. All rights reserved.