期刊
JOURNAL OF MOLECULAR STRUCTURE
卷 1228, 期 -, 页码 -出版社
ELSEVIER
DOI: 10.1016/j.molstruc.2020.129442
关键词
Acetylcholinesterase; Butyrylcholinesterase; N-heterocyclic carbene; PEPPSI complex; X-ray diffraction; alpha-Glycosidase
资金
- Inonu University (Turkey) Research Fund [IUBAP: 2015/10]
- Dokuz Eylul University [2010.KB.FEN.13]
New benzimidazole-functionalized Pd-based complexes bearing N-propylphthalimide group were synthesized and showed inhibitory effects on various enzymes, with similar inhibition profiles.
Herein, six new benzimidazole-functionalized Pd-based complexes bearing N-propylphthalimide group were synthesized. These new PEPPSI type of Pd(II)NHC complexes (PEPPSI: Pyridine Enhanced Precatalyst Preparation, Stabilization and Initiation) were prepared from the N-propylphthalimide substituted benzimidazolium salts, palladium chloride (PdCl2) and 3-chloropyridine. The structures of all (NHC)PdX2(3-chloropyridine) complexes have been clearly characterized by using NMR (H-1 and C-13), FTIR spectroscopic method, and elemental analysis techniques. Also, the structures of three of the (NHC)PdX2(3-chloropyridine) complexes were confirmed by single-crystal X-ray diffraction. Also, novel N-propylphthalimide-substituted (NHC)PdX 2 (3-chloropyridine) complexes effectively inhibited acetylcholinesterase (AChE), with Ki values in the range of 0.54 +/- 0.10 to 3.01 +/- 0.63 mu M. For butyryl-cholinesterase (BChE) was obtained with Ki values in the range of 0.82 +/- 0.11 to 5.03 +/- 0.86 mu M. For alpha-glycosidase (alpha-Gly) the most effective Ki values of 1c, 1d, and 1b were with Ki values of 23.83 +/- 5.98, 26.04 +/- 7.11, and 30.61 +/- 3.85 mu M, respectively. All novel N-propylphthalimide-substituted PEPPSI complexes and control compounds had almost similar inhibition profiles. (C) 2020 Elsevier B.V. All rights reserved.
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