期刊
HELIYON
卷 8, 期 9, 页码 -出版社
CELL PRESS
DOI: 10.1016/j.heliyon.2022.e10625
关键词
Acetylcholinesterase; Bio-catalysis; NHC; Palladium complexes; PEPPSI; Single crystal; Carbonic anhydrases
资金
- Dokuz Eylul University for the use of the Oxford Rigaku Xcalibur Eos Diffractometer [2010.KB.FEN.13]
This study reports the synthesis of a series of palladium-based complexes bearing N-heterocyclic carbene (NHC) ligand, characterizes their properties and structures, and investigates their inhibition effects on biological enzymes.
The palladium-based complexes bearing N-heterocyclic carbene (NHC) ligand have long attracted attention as active catalysts for many catalytic reactions. Recently, the biological activities of these complexes, which are stable to air and moisture, have also been wondered. With the aim, we report the synthesis of a series of (NHC) Pd(Br2)(L) complexes (NHC: 1,3-dibenzylbenzimidazolium, L: morpholine, triphenylphosphine, pyridine, 3-chloropyridine, and 2-aminopyridine). All complexes were characterized by NMR (1H and 13C), FTIR spectroscopic and elemental analysis techniques. In addition, the single crystal structures of the complex 3, 4, and 6 were determined through single crystal x-ray crystallographic method. Furthermore, the carbonic anhydrase I and II isoenzymes (hCAs) and acetylcholinesterase (AChE) inhibition effects of these palladium-based complexes bearing NHC ligand were investigated. They showed highly potent inhibition effect with Ki values are between 10.06 +/- 1.49-68.56 +/- 11.53 nM for hCA I isoenzyme, 7.74 +/- 0.66 to 49.39 +/- 6.50 nM for hCA II isoenzyme and 22.83 +/- 3.21 to 64.09 +/- 9.05 nM for AChE enzyme.
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