Synthesis,crystal structure and biological evaluation of spectroscopic characterization of Ni(II) and Co(II) complexes with N‐salicyloil‐N′‐maleoil‐hydrazine as anticholinergic and antidiabetic agents |
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Authors: | Gulnar Gondolova Parham Taslimi Ajdar Medjidov Vagif Farzaliyev Afsun Sujayev Mansura Huseynova Onur Şahin Bahattin Yalçın Fikret Turkan İlhami Gulçin |
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Affiliation: | 1. Department of the Azerbaijan National Academy of Sciences, Institute of Ecology and Natural Resources, Ganja, Azerbaijan;2. Department of Chemistry, Faculty of Sciences, Ataturk University, Erzurum, Turkey;3. Department of “Coordination compounds”, Institute of Catalysis and Inorganic Chemistry Azerbaijan National Academy of Sciences, Baku, Azerbaijan;4. Laboratory of Theoretical Bases of Synthesis and Action Mechanism of Additives, Institute of Chemistry of Additives, Azerbaijan National Academy of Sciences, Baku, Azerbaijan;5. Institute of Chemistry of Additives, Azerbaijan National Academy of Sciences, Baku, Azerbaijan;6. Scientific and Technological Research Application and Research Center, Sinop University, Sinop, Turkey;7. Department of Chemistry, Faculty of Arts Sciences, Marmara University, Istanbul, Turkey;8. Health Services Vocational School, Igd?r University, Igd?r, Turkey |
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Abstract: | [Ni(C11H9N2O5)2(H2O)2]?3(C3H7NO) ( 1 ) and [Co(C11H9N2O5)2(H2O)2]?3(C3H7NO) ( 2 ) are synthesized and characterized by elemental analysis, FT‐IR spectra, magnetic susceptibility, and thermal analysis. In addition, the crystal structure of Ni(II) complex is presented. Both complexes show distorted octahedral geometry. In 1 and 2, metal ions are coordinated by two oxygen atoms of salicylic residue and two nitrogen atoms of maleic amide residue from two ligands, and two oxygen atoms from two water molecules. In this paper, both compounds showed excellent inhibitory effects against human carbonic anhydrase (hCA) isoforms I, and II, α‐glycosidase, acetylcholinesterase (AChE), and butyrylcholinesterase (BChE). Compounds 1 and 2 had Ki values of 18.36 ± 4.38 and 26.61 ± 7.54 nM against hCA I and 13.81 ± 3.02 and 29.56 ± 6.52 nM against hCA II, respectively. On the other hand, their Ki values were found to be 487.45 ± 54.18 and 453.81 ± 118.61 nM against AChE and 199.21 ± 50.35 and 409.41 ± 6.86 nM against BChE, respectively. |
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Keywords: | crystal structure enzyme inhibition magnetic properties N‐salicyloil‐N’ ‐maleoil‐hydrazine synthesis |
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