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<p>5-alkyl/aryl-4-(3,4,5-trimethoxyphenyl)-2,4-dihydro-3H-1,2,4-triazol-3-ones (2a-2f) were synthesized and confirmed by FTIR, <sup>1</sup>H- and <sup>13</sup>C-NMR spectroscopic methods. The details of molecular structure the compounds were investigated by DFT calculations. All the theoretical study was carried out at DFT/B3LYP/6–311 +  + G(d,p) level. The optimized geometries, IR and NMR specral data, MEP maps of compounds 2a-2f were obtained theoretically. The spectral data were compared with the experimental ones and the molecular structures of compounds were investigated in detailed. The results indicate the presence of strong intermolecular hydrogen bonds of N–H⋅⋅O type in the molecular structure of compounds 2a-2f. The biological evaluation demonstrated that all compounds exhibited antimicrobial activity with MIC values ranging from 156 to 1250&#xa0;µg/mL. In particular, compounds 2c, 2d, and 2f showed the strongest antifungal effects against <i>Candida albicans</i> (MIC = 156&#xa0;µg/mL), while compounds 2a, 2b, and 2e also showed moderate antifungal activity (MIC = 312&#xa0;µg/mL). Compound 2b further exhibited the most potent acetylcholinesterase (AChE) inhibitory activity (IC₅₀ = 13&#xa0;µM) among the series. These findings identify compound 2b as a promising dual-activity molecule with both AChE inhibitory and antimicrobial properties. Compounds were also tested for their biological activities, the antimicrobial screening indicated that compounds 2c, 2d, and 2f exhibited moderate inhibitory activity, particularly against <i>Candida albicans</i>. Compound 2b showed the highest acetylcholinesterase (AChE) inhibitory activity among the series, with an IC₅₀ value of 13&#xa0;µM. Moreover, molecular docking and molecular dynamics simulations were performed to investigate the binding interactions between the newly synthesized compound 2b and human acetylcholinesterase (hAChE).&#xa0;</p>

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Trimethoxyphenyl-1,2,4-triazol-3-ones: synthesis, characterization, DFT, antimicrobial and acetylcholinesterase inhibitory activities with molecular docking and dynamics studies

  • 期刊论文

  • 发表日期：

    2025年8月29日

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  • Yasemin Ünver,
  • Fatih Çelik,
  • Halil İbrahim Güler,
  • Kadriye İnan Bektaş,
  • Nevin Süleymanoğlu,
  • Reşat Ustabaş

摘要

5-alkyl/aryl-4-(3,4,5-trimethoxyphenyl)-2,4-dihydro-3H-1,2,4-triazol-3-ones (2a-2f) were synthesized and confirmed by FTIR, 1H- and 13C-NMR spectroscopic methods. The details of molecular structure the compounds were investigated by DFT calculations. All the theoretical study was carried out at DFT/B3LYP/6–311 +  + G(d,p) level. The optimized geometries, IR and NMR specral data, MEP maps of compounds 2a-2f were obtained theoretically. The spectral data were compared with the experimental ones and the molecular structures of compounds were investigated in detailed. The results indicate the presence of strong intermolecular hydrogen bonds of N–H⋅⋅O type in the molecular structure of compounds 2a-2f. The biological evaluation demonstrated that all compounds exhibited antimicrobial activity with MIC values ranging from 156 to 1250 µg/mL. In particular, compounds 2c, 2d, and 2f showed the strongest antifungal effects against Candida albicans (MIC = 156 µg/mL), while compounds 2a, 2b, and 2e also showed moderate antifungal activity (MIC = 312 µg/mL). Compound 2b further exhibited the most potent acetylcholinesterase (AChE) inhibitory activity (IC₅₀ = 13 µM) among the series. These findings identify compound 2b as a promising dual-activity molecule with both AChE inhibitory and antimicrobial properties. Compounds were also tested for their biological activities, the antimicrobial screening indicated that compounds 2c, 2d, and 2f exhibited moderate inhibitory activity, particularly against Candida albicans. Compound 2b showed the highest acetylcholinesterase (AChE) inhibitory activity among the series, with an IC₅₀ value of 13 µM. Moreover, molecular docking and molecular dynamics simulations were performed to investigate the binding interactions between the newly synthesized compound 2b and human acetylcholinesterase (hAChE).