((E)-N′(3,5-di-tert-butil-2-hedroxybenzilidene)-2-hydroxybenzohydrazide (H3sahz)2 Copper (II) Complex: Synthesis, Crystal Structures, in silico Evaluations, and Enzymatic Inhibition

Fatullayeva P. A., Mejidov A. A., Safronenko M. G., Nikolayevich Khrustalev V., Yalcin B., Sadeghian N., ...Daha Fazla

ChemistrySelect, cilt.8, sa.15, 2023 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 8 Sayı: 15
  • Basım Tarihi: 2023
  • Doi Numarası: 10.1002/slct.202300319
  • Dergi Adı: ChemistrySelect
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier
  • Anahtar Kelimeler: Bioactivity, Enzymes inhibition, Molecular Docking, Salicylic acid hydrazide, X-ray, CU(II), DESIGN, LEAVES
  • Marmara Üniversitesi Adresli: Evet

Özet

In this study, (E)-N′(3,5-di-tert-butil-2-hedroxybenzilidene)-2-hydroxybenzohydrazide (H3sahz)2 and its copper (II) complex has been synthesized and evaluated by methods FTIR, UV–Vis, EPR, and single crystal X-ray analysis. It has been shown, that H3sahz crystallizes as a dimer through hydrogen bonds. H3sahz with copper nitrate forms [Cu(H2sahz)(NO3)(H2O)] complex, which according to X-ray diffraction analysis has a distorted square pyramidal structure. The complex was screened for α-glucosidase (α-Glu), acetylcholinesterase (AChE), and butyrylcholinesterase (BChE) inhibitory abilities. Results displayed that IC50 and Ki values of the novel complex for AChE, BChE, and α-Glu enzymes were obtained at 0.93–2.14, 1.01–2.03, and 73.86–102.65 μM, respectively. The molecular docking outcomes have shown that the synthetic complex has a lower affinity for α-glucosidase compared to acarbose. But the inhibition ability of H3sahz for acetylcholinesterase and butyrylcholinesterase enzymes was greater than that of tacrine. These findings indicate that the (H3sahz)2 complex may be considered a possible candidate for the development and discovery of compounds effective in inhibiting the relevant enzymes.