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

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作者：

Qurrat-ul-Ain,，U Ashiq，RA Jamal，M Saleem，M Mahroof-Tahir

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摘要：

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 α-glucosidase and carbonic anhydrase II enzyme inhibition activities. The physical, analytical (elemental analyses for C, H, N and Pd) and spectral (FT-IR, 1H NMR, 13C 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 α-glucosidase and carbonic anhydrase II enzymes; however, the respective Pd(II)-hydrazide complexes were approximately 300 times more potent α-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).

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关键词：

Pd(II) complexes Hydrazide α-Glucosidase Carbonic anhydrase Enzyme

DOI：

10.1016/j.arabjc.2015.02.024

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年份：

2015