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<p>Ten halogenated benzofuran derivatives (BF1–BF10) were synthesized and evaluated for their inhibitory activity against monoamine oxidase isoforms. All compounds showed stronger inhibition of MAO-B compared to MAO-A. Among them, BF2 exhibited the most potent MAO-B inhibition (IC₅₀ = 0.082 µM), followed by BF5 (IC₅₀ = 0.095 µM) and BF1 (IC₅₀ = 0.16 µM), with high selectivity indices, particularly BF2 (SI = 1038.05). Kinetic studies revealed that BF2 acts as a competitive inhibitor with a K<sub>i</sub> value of 0.083 ± 0.0056 µM. Dialysis experiments confirmed its reversible inhibition profile, comparable to the reference drug Safinamide. Both BF2and BF5 were non-cytotoxic toward L929 cells and demonstrated moderate blood–brain barrier permeability in PAMPA assay. Molecular docking showed stabilization of MAO-B via π–π stacking interactions with Tyr326 and Tyr398, and molecular dynamics simulations further confirmed stable binding of BF2 within the MAO-B active site. Overall, BF2 emerged as a potent, selective, and reversible MAO-B inhibitor, warranting for further investigation.</p>

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Development of 1-(substituted benzofuran-2-yl)-3-(halogen-substituted phenyl)prop-2-en-1-ones as potent, reversible, and selective MAO-B inhibitors for Parkinson’s Disease

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年6月3日

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  • Ali Hasan,
  • Jiseong Lee,
  • Naresh Payyaula,
  • Vishnu Vasanthi Radhakrishanan,
  • Sachithra Thazhathuveedu Sudevan,
  • Sunil Kumar,
  • Della Grace Thomas Parambi,
  • Kasim Sakran Abass,
  • Arun Kumar,
  • Naseer Maliyakkal,
  • Hoon Kim,
  • Bijo Mathew

摘要

Ten halogenated benzofuran derivatives (BF1–BF10) were synthesized and evaluated for their inhibitory activity against monoamine oxidase isoforms. All compounds showed stronger inhibition of MAO-B compared to MAO-A. Among them, BF2 exhibited the most potent MAO-B inhibition (IC₅₀ = 0.082 µM), followed by BF5 (IC₅₀ = 0.095 µM) and BF1 (IC₅₀ = 0.16 µM), with high selectivity indices, particularly BF2 (SI = 1038.05). Kinetic studies revealed that BF2 acts as a competitive inhibitor with a Ki value of 0.083 ± 0.0056 µM. Dialysis experiments confirmed its reversible inhibition profile, comparable to the reference drug Safinamide. Both BF2and BF5 were non-cytotoxic toward L929 cells and demonstrated moderate blood–brain barrier permeability in PAMPA assay. Molecular docking showed stabilization of MAO-B via π–π stacking interactions with Tyr326 and Tyr398, and molecular dynamics simulations further confirmed stable binding of BF2 within the MAO-B active site. Overall, BF2 emerged as a potent, selective, and reversible MAO-B inhibitor, warranting for further investigation.