Alpha-glucosidase and carbonic anhydrase inhibition studies of Pd(II)-hydrazide complexes

作者：Qurrat ul Ain; Ashiq Uzma; Jamal Rifat Ara; Saleem Muhammad; Mahroof Tahir Mohammad^*

来源：Arabian Journal of Chemistry, 2017, 10(4): 488-499.

DOI：10.1016/j.arabjc.2015.02.024

• Pd(II) complexes
• Hydrazide
• alpha-Glucosidase
• Carbonic anhydrase
• Enzyme

This study focused on the synthesis and characterization of hydrazide ligands and their respective Pd(II) complexes and used high throughput screening to determine their a-glucosidase and carbonic anhydrase II enzyme inhibition activities. The physical, analytical (elemental analyses for C, H, N and Pd) and spectral (FT-IR, H-1 NMR, C-13 NMR, EI-mass) techniques utilized during characterization revealed the formation of square planar, neutral and 1: 2 Pd(II)-hydrazide complexes with the general formula [PdL2Cl2]. In these Pd(II) complexes, the hydrazide ligands are monodentate; the terminal nitrogen is the donor atom. The uncoordinated hydrazide ligands were inactive against both alpha-glucosidase and carbonic anhydrase II enzymes; however, the respective Pd(II)-hydrazide complexes were approximately 300 times more potent alpha-glucosidase inhibitors than the standard compound, 1-deoxynojirimycin (DNJ). Some of the Pd(II) complexes also demonstrated potential carbonic anhydrase (CA) inhibition properties comparable to the standard compound, acetazolamide (ACZ).

• 出版日期2017-5