Erdemir_2019_Bioorg.Chem_91_103134

In this work, the synthesis, crystal structure, characterization, and enzyme inhibition effects of the novel a series of 2-aminopyridine liganded Pd(II) N-heterocyclic carbene (NHC) complexes were examined. These complexes of the Pd-based were synthesized from PEPPSI complexes and 2-aminopyridine. The novel complexes were characterized by using (13)C NMR, (1)H NMR, elemental analysis, and FTIR spectroscopy techniques. Also, crystal structures of the two compounds were recorded by using single-crystal X-ray diffraction assay. Also, these complexes were tested toward some metabolic enzymes like alpha-glycosidase, aldose reductase, butyrylcholinesterase, acetylcholinesterase enzymes, and carbonic anhydrase I, and II isoforms. The novel 2-aminopyridine liganded (NHC)PdI2(2-aminopyridine) complexes (1a-i) showed Ki values of in range of 5.78+/-0.33-22.51+/-8.59nM against hCA I, 13.77+/-2.21-30.81+/-4.87nM against hCA II, 0.44+/-0.08-1.87+/-0.11nM against AChE and 3.25+/-0.34-12.89+/-4.77nM against BChE. Additionally, we studied the inhibition effect of these derivatives on aldose reductase and alpha-glycosidase enzymes. For these compounds, compound 1d showed maximum inhibition effect against AR with a Ki value of 360.37+/-55.82nM. Finally, all compounds were tested for the inhibition of alpha-glycosidase enzyme, which recorded efficient inhibition profiles with Ki values in the range of 4.44+/-0.65-12.67+/-2.50nM against alpha-glycosidase.