Novel 2-aminopyridine liganded Pd(II) N-heterocyclic carbene complexes: Synthesis, characterization, crystal structure and bioactivity properties


Erdemir P., Celepci D. B. , AKTAŞ A. , GÖK Y. , Kaya R., Taslimi P., ...Daha Fazla

BIOORGANIC CHEMISTRY, cilt.91, 2019 (SCI İndekslerine Giren Dergi) identifier identifier identifier

Özet

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 C-13 NMR, H-1 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 a-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 +/- 8.59 nM against hCA I, 13.77 +/- 2.21-30.81 +/- 4.87 nM against hCA II, 0.44 +/- 0.08-1.87 +/- 0.11 nM against AChE and 3.25 +/- 0.34-12.89 +/- 4.77 nM 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 +/- 55.82 nM. 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 +/- 2.50 nM against aglycosidase.