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<p>Xanthine oxidase (XO), a key enzyme in purine metabolism, plays a critical role in hyperuricemia. This study evaluated the inhibitory effects of twenty-four food colorants on XO, with tartrazine (TZ) and sunset yellow (SY) showing significant reversible mixed inhibition (IC<sub>50</sub> = 71.71 ± 0.05 µM and 87.27 ± 0.01 µM, respectively). Synchronous fluorescence spectroscopy analyses revealed distinct interaction mechanisms: TZ increased the polarity around tryptophan residues, whereas SY enhanced tyrosine hydrophobicity. Thermodynamic and fluorescence quenching assays indicated spontaneous, hydrophobic-driven binding. Circular dichroism confirmed structural changes in XO, with decreased <i>α</i>-helix and increased <i>β</i>-strands/random coils upon binding. Docking studies identified key residues (TZ: Trp1116, Leu1098, Leu1054, Pro1057, and Ile1056; SY: Phe418, Glu332, Ser419, Lys526 and Phe421) involved in hydrophobic interactions. These findings provided insights into the underlying molecular of the anti-gout properties with TZ and SY, and supporting further exploration of food colorants as XO inhibitors.</p>

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Insights Into the Inhibitory Activity and Mechanism of Food Colorants Tartrazine and Sunset Yellow on Xanthine Oxidase by Multiple Spectroscopic Techniques and Molecular Docking

  • 期刊论文

  • 发表日期：

    2025年6月25日

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  • Jiaying Ma,
  • Xiaoyue Dong,
  • Lu Wang,
  • Shaohua Sun,
  • Zhongbai Shao,
  • Hui Wang,
  • Shiwei Sun,
  • Wei Wang

摘要

Xanthine oxidase (XO), a key enzyme in purine metabolism, plays a critical role in hyperuricemia. This study evaluated the inhibitory effects of twenty-four food colorants on XO, with tartrazine (TZ) and sunset yellow (SY) showing significant reversible mixed inhibition (IC50 = 71.71 ± 0.05 µM and 87.27 ± 0.01 µM, respectively). Synchronous fluorescence spectroscopy analyses revealed distinct interaction mechanisms: TZ increased the polarity around tryptophan residues, whereas SY enhanced tyrosine hydrophobicity. Thermodynamic and fluorescence quenching assays indicated spontaneous, hydrophobic-driven binding. Circular dichroism confirmed structural changes in XO, with decreased α-helix and increased β-strands/random coils upon binding. Docking studies identified key residues (TZ: Trp1116, Leu1098, Leu1054, Pro1057, and Ile1056; SY: Phe418, Glu332, Ser419, Lys526 and Phe421) involved in hydrophobic interactions. These findings provided insights into the underlying molecular of the anti-gout properties with TZ and SY, and supporting further exploration of food colorants as XO inhibitors.