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Transition‐Metal Complexes of Bidentate Schiff‐Base Ligands: In Vitro and In Silico Evaluation as Non‐Classical Carbonic Anhydrase and Potential Acetylcholinesterase Inhibitors
Author(s) -
Yaşar Ümit,
Gönül İlyas,
Türkeş Cüneyt,
Demir Yeliz,
Beydemir Şükrü
Publication year - 2021
Publication title -
chemistryselect
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.437
H-Index - 34
ISSN - 2365-6549
DOI - 10.1002/slct.202102082
Subject(s) - carbonic anhydrase , chemistry , denticity , schiff base , acetylcholinesterase , carbonic anhydrase i , carbonic anhydrase ii , isozyme , stereochemistry , active site , enzyme , docking (animal) , metal , in silico , medicinal chemistry , biochemistry , organic chemistry , gene , medicine , nursing
Schiff bases display superior features for many areas, such as significant intermediates in industrial biological, pharmacological, catalytic and optical properties, organic synthesis, and coordination chemistry. The pre‐synthesized two Schiff base ligands ( HL 1 and HL 2 ) and their bidentate metal complexes ( Co(L 1 ) 2 , Cu ( L 1 ) 2 , Ni ( L 1 ) 2 , Co(L 2 ) 2 , Cu ( L 2 ) 2 , and Ni ( L 2 ) 2 ) were tested for their inhibition activities on acetylcholinesterase (AChE) and human carbonic anhydrase ( h CA I and h CA II) isoforms. The transition metal complexes of bidentate Schiff base ligands displayed the potent inhibition effect with K I constants ranging from 16.39±0.15 to 88.63±0.27 nM and 9.32±0.13 to 33.66±0.57 nM for h CA isoenzymes and AChE, respectively. The compound Cu ( L 1 ) 2 for h CA I and Ni ( L 2 ) 2 for AChE and h CA II had the highest inhibitory effect. Besides, the molecular docking analyses of the most active complexes ( Cu ( L 1 ) 2 and Ni ( L 2 ) 2 ) were performed to understand the binding interactions on the enzymes’ binding sites. According to both in vitro and in silico analysis results, all the compounds were potential inhibitors of AChE and h CA I, II isoenzymes.