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Comparative study on the interaction between flavonoids with different core structures and hyaluronidase.

Xiangrong Li1, Ruonan Xu1, Zeqing Cheng2

  • 1Department of Medical Chemistry, Key Laboratory of Medical Molecular Probes, School of Basic Medicine, Xinxiang Medical University, Xinxiang, Henan 453003, PR China.

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Summary

Flavonoids inhibit hyaluronidase (HAase) activity by binding to the enzyme, with rutin showing the strongest affinity. This interaction, driven by hydrophobic and electrostatic forces, suggests a potential anti-inflammatory mechanism for these natural compounds.

Keywords:
FlavonoidsInteractionSpectroscopy

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Area of Science:

  • Biochemistry
  • Pharmacology

Background:

  • Hyaluronidase (HAase) is a key enzyme in inflammatory pathways.
  • Flavonoids, a class of polyphenols, exhibit known anti-inflammatory properties.

Purpose of the Study:

  • To investigate the binding interactions between six flavonoids and HAase.
  • To elucidate the mechanism of HAase inhibition by flavonoids.

Main Methods:

  • Steady-state and time-resolved fluorescence spectroscopy.
  • Circular dichroism (CD) spectroscopy.
  • Molecular docking simulations.

Main Results:

  • All tested flavonoids induced static quenching of HAase fluorescence.
  • Rutin demonstrated the highest binding affinity, followed by hesperidin, myricetin, puerarin, genistein, and naringin.
  • Flavonoid binding involves hydrophobic interactions, electrostatic forces, and hydrogen bonding, altering the enzyme's microenvironment and secondary structure.

Conclusions:

  • Flavonoids bind to HAase, potentially inhibiting its activity.
  • The study provides insights into the molecular mechanisms underlying the anti-inflammatory effects of flavonoids.
  • Rutin shows significant potential as an HAase inhibitor.