<p>In this study, tetrahydronaphthalene carbothioamides <b>2</b>, characterized by spectroscopic methods and X-ray diffraction studies, were used to develop a series of novel tetrahydronaphthalenone-coupled thiazole derivatives <b>3</b>. The synthesized thiazole hybrids were evaluated for in-vitro anti-inflammatory activity against lipopolysaccharide (LPS)-induced inflammation in RAW264.7 macrophage cells. Notably, compound <b>3f</b> demonstrated the most potent anti-inflammatory effect by significantly reducing the expression of pro-inflammatory mediators, including nitric oxide species (IC<sub>50</sub> = 62.93&#xa0;µM) and tumor necrosis factor-α (TNF-α) (67.50&#xa0;µM). Additionally, <b>3f</b> inhibited cyclooxygenase-2 (COX-2) (IC<sub>50</sub> = 73.18&#xa0;µM compared to celecoxib 41.21&#xa0;µM) expression in a dose-dependent manner. The antioxidant activity of newly generated derivatives was also assessed using the DPPH assay, with compounds <b>3a</b>, <b>3b</b>, and <b>3c</b> showing the highest inhibition rates of 69.94%, 68.82%, and 64.77% at 100&#xa0;µg/mL, respectively. Molecular docking studies targeting the active site of Human Peroxiredoxin 5 (PDB ID: 1HD2) and COX-2 (PDB ID: 4M11) were conducted to explore the potential interactions of these compounds with the receptor. Molecular dynamics (MD) simulation predicted the stability of the protein–ligand complex.</p>

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Exploration of naphthalenone-thiazole hybrids for TNF-α, COX-2 inhibition and anti-oxidant capability

  • Jyoti Yadav,
  • R. P. Chaudhary

摘要

In this study, tetrahydronaphthalene carbothioamides 2, characterized by spectroscopic methods and X-ray diffraction studies, were used to develop a series of novel tetrahydronaphthalenone-coupled thiazole derivatives 3. The synthesized thiazole hybrids were evaluated for in-vitro anti-inflammatory activity against lipopolysaccharide (LPS)-induced inflammation in RAW264.7 macrophage cells. Notably, compound 3f demonstrated the most potent anti-inflammatory effect by significantly reducing the expression of pro-inflammatory mediators, including nitric oxide species (IC50 = 62.93 µM) and tumor necrosis factor-α (TNF-α) (67.50 µM). Additionally, 3f inhibited cyclooxygenase-2 (COX-2) (IC50 = 73.18 µM compared to celecoxib 41.21 µM) expression in a dose-dependent manner. The antioxidant activity of newly generated derivatives was also assessed using the DPPH assay, with compounds 3a, 3b, and 3c showing the highest inhibition rates of 69.94%, 68.82%, and 64.77% at 100 µg/mL, respectively. Molecular docking studies targeting the active site of Human Peroxiredoxin 5 (PDB ID: 1HD2) and COX-2 (PDB ID: 4M11) were conducted to explore the potential interactions of these compounds with the receptor. Molecular dynamics (MD) simulation predicted the stability of the protein–ligand complex.