RESUMO
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 13C NMR, 1H 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 α-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⯱â¯0.33-22.51⯱â¯8.59â¯nM against hCA I, 13.77⯱â¯2.21-30.81⯱â¯4.87â¯nM against hCA II, 0.44⯱â¯0.08-1.87⯱â¯0.11â¯nM against AChE and 3.25⯱â¯0.34-12.89⯱â¯4.77â¯nM against BChE. Additionally, we studied the inhibition effect of these derivatives on aldose reductase and α-glycosidase enzymes. For these compounds, compound 1d showed maximum inhibition effect against AR with a Ki value of 360.37⯱â¯55.82â¯nM. Finally, all compounds were tested for the inhibition of α-glycosidase enzyme, which recorded efficient inhibition profiles with Ki values in the range of 4.44⯱â¯0.65-12.67⯱â¯2.50â¯nM against α-glycosidase.
