((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
2023; Wiley; Volume: 8; Issue: 15 Linguagem: Inglês
10.1002/slct.202300319
ISSN2365-6549
AutoresP.A. Fatullayeva, Ajdar Akper Mejidov, М. Г. Сафроненко, Victor Nikolayevich Khrustalev, Bahaddin Yalcin, Nastaran Sadeghian, Morteza Sadeghi, Parham Taslımı,
Tópico(s)Metal complexes synthesis and properties
ResumoAbstract In this study, (E)‐N′(3,5‐di‐tert‐butil‐2‐hedroxybenzilidene)‐2‐hydroxybenzohydrazide (H 3 sahz) 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 H 3 sahz crystallizes as a dimer through hydrogen bonds. H 3 sahz with copper nitrate forms [Cu(H 2 sahz)(NO 3 )(H 2 O)] 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 IC 50 and K i 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 H 3 sahz for acetylcholinesterase and butyrylcholinesterase enzymes was greater than that of tacrine. These findings indicate that the (H 3 sahz) 2 complex may be considered a possible candidate for the development and discovery of compounds effective in inhibiting the relevant enzymes.
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