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<p>In the context of research into known synthetic possibilities under the conditions of condensation reaction, based on cobalt salt (Co(CH<sub>3</sub>COO)<sub>2</sub>•4H<sub>2</sub>O) with 3-((1,5-dimethyl-3-oxo-2-phenyl-2,3-dihydro-1&#xa0;H-pyrazol-4-yl)diazenyl)pentane-2,4-dione, metal-complex was synthesized. To assess its interactions with biological targets, a single-crystal X-ray diffraction structure analysis were conducted. It has been revealed that independent part of the unit cell of the cobalt(II) complex contains one complex molecule of composition C<sub>32</sub>H<sub>34</sub>N<sub>8</sub>O<sub>6</sub>Co(II), one molecule of acetic acid anion and five molecules of water of crystallization. All atoms are in a general position. The four O atoms in the equatorial plane around the Co atom form a slightly distorted square-planar arrangement with an average Co-O bond length of 1.888 Å, and the slightly distorted octahedral coordination is completed by the two N atoms of the in the axial positions. Each Co(II)-complexes contain two independent molecules of C<sub>16</sub>H<sub>17</sub>N<sub>4</sub>O<sub>3</sub>. This molecule has pentagonal and hexagonal cyclic fragments. This complex is effective inhibitor of the α-glycosidase, butyrylcholinesterase (BChE), cytosolic carbonic anhydrase I and II isoforms (hCA I and II), and acetylcholinesterase enzymes (AChE) with Ki values of 1.93 ± 0.38 µM for hCA I, 1.85 ± 0.12 µM for hCA II, 6.31 ± 0.47 µM for α-glycosidase, 39.54 ± 8.18 µM for BChE, and 49.85 ± 15.72 µM for AChE, respectively. Afterwards, the interactions of the molecules against various proteins that are structure of α-galactosidase (α-Gly) (PDB ID: 1R47), carbonic anhydrase I (hCA I) (PDB ID: 2CAB), carbonic anhydrase II (hCA II) (PDB ID: 3DC3), acetylcholinesterase (AChE) (PDB ID: 4M0E), and butyrylcholinesterase (BChE) (PDB ID: 5NN0) were examined and their activities were compared.</p>

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Synthesis, single-crystal X-Ray, molecular docking studies, and metabolic enzyme inhibition properties of novel Co(II) metal complex

  • 期刊论文

  • 发表日期：

    2026年2月26日

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  • Famil Chiragov,
  • Kanan Agayev,
  • Faik Musayev,
  • Imamaddin Amiraslanov,
  • Vagif Farzaliyev,
  • Afsun Sujayev,
  • Burak Tüzün,
  • Parham Taslimi,
  • Nastaran Sadeghian,
  • Eda Mehtap Özden,
  • Saleh Alwasel,
  • İlhami Gulçin

摘要

In the context of research into known synthetic possibilities under the conditions of condensation reaction, based on cobalt salt (Co(CH3COO)2•4H2O) with 3-((1,5-dimethyl-3-oxo-2-phenyl-2,3-dihydro-1 H-pyrazol-4-yl)diazenyl)pentane-2,4-dione, metal-complex was synthesized. To assess its interactions with biological targets, a single-crystal X-ray diffraction structure analysis were conducted. It has been revealed that independent part of the unit cell of the cobalt(II) complex contains one complex molecule of composition C32H34N8O6Co(II), one molecule of acetic acid anion and five molecules of water of crystallization. All atoms are in a general position. The four O atoms in the equatorial plane around the Co atom form a slightly distorted square-planar arrangement with an average Co-O bond length of 1.888 Å, and the slightly distorted octahedral coordination is completed by the two N atoms of the in the axial positions. Each Co(II)-complexes contain two independent molecules of C16H17N4O3. This molecule has pentagonal and hexagonal cyclic fragments. This complex is effective inhibitor of the α-glycosidase, butyrylcholinesterase (BChE), cytosolic carbonic anhydrase I and II isoforms (hCA I and II), and acetylcholinesterase enzymes (AChE) with Ki values of 1.93 ± 0.38 µM for hCA I, 1.85 ± 0.12 µM for hCA II, 6.31 ± 0.47 µM for α-glycosidase, 39.54 ± 8.18 µM for BChE, and 49.85 ± 15.72 µM for AChE, respectively. Afterwards, the interactions of the molecules against various proteins that are structure of α-galactosidase (α-Gly) (PDB ID: 1R47), carbonic anhydrase I (hCA I) (PDB ID: 2CAB), carbonic anhydrase II (hCA II) (PDB ID: 3DC3), acetylcholinesterase (AChE) (PDB ID: 4M0E), and butyrylcholinesterase (BChE) (PDB ID: 5NN0) were examined and their activities were compared.