In Silico and In Vitro Analysis of Acetylcholinesterase and Glutathione S-Transferase Enzymes of Substituted Pyrazoles

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Cetin A., Oğuz E., Türkan F.

RUSSIAN JOURNAL OF GENERAL CHEMISTRY, cilt.92, sa.11, ss.2415-2428, 2022 (SCI-Expanded)

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 92 Sayı: 11
  • Basım Tarihi: 2022
  • Doi Numarası: 10.1134/s1070363222110263
  • Dergi Adı: RUSSIAN JOURNAL OF GENERAL CHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED)
  • Sayfa Sayıları: ss.2415-2428
  • Van Yüzüncü Yıl Üniversitesi Adresli: Evet

Özet

A series of substitute pyrazole compounds including azide, acetyl, triazole, morpholine, piperidine, and pyrrolidine moieties were synthesized and their structures were elucidated by NMR, HPLC and mass spectroscopy. The inhibition efficiencies of all novel compounds against acetylcholinesterase (AChE) and glutathione S-transferase (GST) enzymes were investigated. In vitro studies revealed that the inhibitory activities of substitute pyrazole compounds were determined with Ki values in the range of 0.11–0.49 µM for AChE, and 0.12–0.91 µM for GST, respectively. Furthermore, the molecular docking studies of the detailed interactions between the pyrazole compounds and AChE-GST enzymes were identified with bonding type, distance, hydrophobic bonds and hydrogen bonds. The binding energies of the AChE-pyrazole analogs’ complexes were found between –5.5 and –9.3 kcal/mol, and the binding energies of the GST-pyrazole analogs’ complexes were found between –5.9 and –9.2 kcal/mol.