Synthesis, characterization, crystal structure and bioactivity properties of the benzimidazole-functionalized PEPPSI type of Pd(II)NHC complexes
Küçük Resim Yok
Tarih
2021
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Elsevier
Erişim Hakkı
info:eu-repo/semantics/closedAccess
Özet
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.
Açıklama
Anahtar Kelimeler
Acetylcholinesterase, Butyrylcholinesterase, N-heterocyclic carbene, PEPPSI complex, X-ray diffraction, alpha-Glycosidase
Kaynak
Journal of Molecular Structure
WoS Q Değeri
Q3
Scopus Q Değeri
Q2
Cilt
1228
