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<p>The effect of anionic dinitrosyl iron complex (DNIC) with 5-(3-pyridyl)-4<i>H</i>-1,2,4-triazole-3-thiolyl (complex <b>1</b>) on cyclooxygenase-2 (COX-2, enzyme induced by inflammatory stimuli and cytokines) was examined. Complex <b>1</b> was found to be an efficient inhibitor of COX-2 functions, which provides its prospects for further study as a potential anti-inflammatory drug. The interaction of complex <b>1</b> with serum albumin, which is the basic blood carrier protein, was studied. In the presence of albumin, NO generation by complex <b>1</b> becomes more prolonged than that in a buffer solution, while the formation of a high-molecular-weight protein-bound dinitrosyl complex is observed in the system. The Stern—Volmer constant was calculated: <i>K</i><sub>SV</sub> = 5.4•10<sup>5</sup> L mol<sup>−1</sup>. Molecular docking shows that DNIC binding to the protein occurs at the junction of three protein domains, and the lowest energy positions of anionic complex <b>1</b> are located in subdomain Ib from the side of domain III surrounded by positively charged side groups of lysine 114 and arginines 144, 185, and 458.</p>

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Dinitrosyl 5-(3-pyridyl)-4H-1,2,4-triazole-3-thiolyl iron complex as a promising anti-inflammatory agent: influence on cyclooxygenase-2 and interaction with serum albumin

  • 期刊论文

  • 发表日期：

    2025年7月1日

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  • L. M. Mazina,
  • O. V. Pokidova,
  • V. B. Luzhkov,
  • K. S. Ruina,
  • N. A. Sanina

摘要

The effect of anionic dinitrosyl iron complex (DNIC) with 5-(3-pyridyl)-4H-1,2,4-triazole-3-thiolyl (complex 1) on cyclooxygenase-2 (COX-2, enzyme induced by inflammatory stimuli and cytokines) was examined. Complex 1 was found to be an efficient inhibitor of COX-2 functions, which provides its prospects for further study as a potential anti-inflammatory drug. The interaction of complex 1 with serum albumin, which is the basic blood carrier protein, was studied. In the presence of albumin, NO generation by complex 1 becomes more prolonged than that in a buffer solution, while the formation of a high-molecular-weight protein-bound dinitrosyl complex is observed in the system. The Stern—Volmer constant was calculated: KSV = 5.4•105 L mol−1. Molecular docking shows that DNIC binding to the protein occurs at the junction of three protein domains, and the lowest energy positions of anionic complex 1 are located in subdomain Ib from the side of domain III surrounded by positively charged side groups of lysine 114 and arginines 144, 185, and 458.