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<p>In this study, we report the design, synthesis, and anti-proliferative effects of 1<i>H</i>-1,2,3-triazole-linked indolin-2-one-bis(thiosemicarbazone/semicarbazones) against estrogen-responsive (MCF-7) and triple-negative (MDA-MB-231) breast cancer cells. Notably, compound <b>6b</b>, featuring F-substitution at the C-5 position of indole and thiosemicarbazone, exhibited a notable IC<sub>50</sub> value of 71.65&#xa0;μM against MCF-7 cells and displayed non-cytotoxicity towards normal kidney cells. To unravel its potential mechanism of action, molecular docking and electrochemical studies were conducted. Electrochemical analysis revealed the compound’s ability to chelate Fe(III), a component present in the active site of ribonucleotide reductase. Furthermore, <b>6b</b> displayed significant binding affinity at the active site of ribonucleotide reductase, as indicated by molecular docking. These collective findings suggest that compound <b>6b</b> holds promise as a potential inhibitor of ribonucleotide reductase.</p>

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Customizing Indolin-2-One-Thiosemicarbazones: Design, Synthesis, Anti-proliferative Assessment Along with In Silico and Electrochemical Investigations

  • 期刊论文

  • 发表日期：

    2025年4月15日

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  • Preeti,
  • Bharvi Sharma,
  • Sarbjeet Kaur,
  • Shanen Perumal,
  • Gabriella Palma,
  • Mandeep Kaur,
  • Inderpreet Kaur,
  • Vipan Kumar

摘要

In this study, we report the design, synthesis, and anti-proliferative effects of 1H-1,2,3-triazole-linked indolin-2-one-bis(thiosemicarbazone/semicarbazones) against estrogen-responsive (MCF-7) and triple-negative (MDA-MB-231) breast cancer cells. Notably, compound 6b, featuring F-substitution at the C-5 position of indole and thiosemicarbazone, exhibited a notable IC50 value of 71.65 μM against MCF-7 cells and displayed non-cytotoxicity towards normal kidney cells. To unravel its potential mechanism of action, molecular docking and electrochemical studies were conducted. Electrochemical analysis revealed the compound’s ability to chelate Fe(III), a component present in the active site of ribonucleotide reductase. Furthermore, 6b displayed significant binding affinity at the active site of ribonucleotide reductase, as indicated by molecular docking. These collective findings suggest that compound 6b holds promise as a potential inhibitor of ribonucleotide reductase.