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<p>A new series of pyrimidopyrimidin-2,4-dione derivatives was created through one-pot multicomponent cyclization reaction combining different aromatic aldehydes such as 3,4-dimethoxybenzaldehyde, 4-hydroxy-3,5-dimethoxybenzaldehyde, 2-hydroxy-1-naphthaldehyde, and 1<i>H</i>-pyrrole-2-carbaldehyde with thiourea and barbituric acid. This was achieved using three reaction methods: either by refluxing the reactants in water using CAN catalyst, under fusion condition, or carrying out the reaction under microwave irradiation as an eco-friendly technique. The synthesized compounds were evaluated for antioxidant and anticancer activities, and the results showed that compound <b>4b</b> has significant activity compared to the other tested compounds. These findings were supported by molecular docking simulation towards the target P53 mutant Y220C protein (PDB ID: 5O1H) which demonstrated favorable interactions with the active receptors.</p>

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Antioxidant, in vitro anticancer and molecular docking of newly synthesized pyrimido[4,5-d]pyrimidine-2,4(1H,3H)-dione derivatives using catalyst and solvent-free one-pot three-component reaction

  • 期刊论文

  • 发表日期：

    2026年7月13日

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  • Eman A. Ghareeb,
  • Naglaa F. H. Mahmoud,
  • Eman A. E. El-Helw

摘要

A new series of pyrimidopyrimidin-2,4-dione derivatives was created through one-pot multicomponent cyclization reaction combining different aromatic aldehydes such as 3,4-dimethoxybenzaldehyde, 4-hydroxy-3,5-dimethoxybenzaldehyde, 2-hydroxy-1-naphthaldehyde, and 1H-pyrrole-2-carbaldehyde with thiourea and barbituric acid. This was achieved using three reaction methods: either by refluxing the reactants in water using CAN catalyst, under fusion condition, or carrying out the reaction under microwave irradiation as an eco-friendly technique. The synthesized compounds were evaluated for antioxidant and anticancer activities, and the results showed that compound 4b has significant activity compared to the other tested compounds. These findings were supported by molecular docking simulation towards the target P53 mutant Y220C protein (PDB ID: 5O1H) which demonstrated favorable interactions with the active receptors.