Document Type : Research Article
Authors
1
Chemistry Department, Art and Science Faculty, Amasya University, Amasya, TURKEY
2
Chemistry Department, Art and Science Faculty, Tokat Gaziosmanpasa University, Tokat, TURKEY
3
Bartin University, Bartin, TURKEY
4
Science Faculty, Department of Chemistry, Cumhuriyet University, Sivas 58140, TURKEY
5
Department of Chemistry, Faculty of Arts and Sciences, Yozgat Bozok University, 66200 Yozgat, TURKEY
Abstract
In this study, new amino acid Schiff base Zn(II) complexes were synthesized. In this context, firstly, new Schiff bases were synthesized from the reaction of 3-methoxy-2-hydroxy benzaldehyde (o-vanillin) and amino acid methyl esters (isoleucine, phenylalanine, methionine). The synthesis of new complexes was carried out by the reaction of these Schiff bases and Zn(OAc)2.2H2O. The structures of the synthesized complexes were elucidated using elemental analysis, FT-IR, NMR, UV-vis and thermal analysis spectroscopy techniques. In this study, novel amino acid schiff base Zn(II) complexes (1a-1c) were synthesized and investigated their effect on some metabolic enzymes such as Acetylcholinesterase (AChE) and Butyrylcholinesterase (BChE). Results indicated that all the molecules exhibited potent inhibitory activities against all targets as compared to the standard inhibitor, revealed by IC50 values. Ki values of compounds for AChE and BChE enzymes were obtained in the ranges 78.04±8.66-111.24±12.61 and 24.31±3.98-85.18±7.05 µM, respectively. Molecular docking calculations have been made to examine the biological activities of metal complexes. Protein Ligand Interaction Profiler (PLIP) was used to examine the chemical interactions of metal complexes with enzymes.
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