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

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    Open Access Version of Record under the terms of the Creative Commons BY-NC-ND license (1.015Mb)
    Date
    2017-05
    Author
    Qurrat-ul-Ain
    Ashiq, Uzma
    Jamal, Rifat Ara
    Saleem, Muhammad
    Mahroof-Tahir, Mohammad
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    Abstract
    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).
    DOI/handle
    http://dx.doi.org/10.1016/j.arabjc.2015.02.024
    http://hdl.handle.net/10576/5546
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    • Chemistry & Earth Sciences [‎614‎ items ]

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