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<p>Protein–polyphenol synergy reshapes functionality, unlocking new applications. Yolk immunoglobulin (IgY), a readily accessible protein derived from eggs, undergoes structural and functional changes upon binding with catechin, which is crucial for expanding its potential uses. This study aims to explore the binding mechanisms, structural alterations, stability changes, and antibacterial properties of the IgY-catechin complex. Using molecular simulation technology, spectroscopy, and antibacterial assays, we investigated the complex in detail. Molecular simulations revealed that catechin binds to key residues (PHE503, THR501, THR505, and GLU511) of IgY, resulting in conformational changes. The predicted free energy of binding was −&#xa0;27.34&#xa0;kJ/mol, primarily driven by hydrogen bonding interactions, with a corresponding binding constant of 1.694 × 10<sup>4</sup> L/mol at 298&#xa0;K. Circular dichroism (CD) analysis a 5.48% decrease in α-helix content, and an increase in random coil content, reflecting structural changes. Moreover, the IgY-catechin complex demonstrated enhanced acid–base stability but slightly reduced thermal stability compared to IgY alone. Fluorescence microscopy and nucleic acid leakage assays confirmed that the complex disrupted the membranes of Escherichia coli and Staphylococcus aureus, leading to the leakage of intracellular genetic material. These findings reveal that the IgY-catechin interaction not only alters the protein structure of IgY but also boosts its antibacterial activity, offering a promising approach to broaden applications in the food industry.</p>

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Polyphenol-driven structural alterations and antibacterial potency of the IgY-catechin complex

  • 期刊论文

  • 发表日期：

    2025年4月30日

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  • Lili Liu,
  • Yanli Wang,
  • Mengjun Zhang,
  • Weiwei Cheng,
  • Yue Ding,
  • Jialiang He

摘要

Protein–polyphenol synergy reshapes functionality, unlocking new applications. Yolk immunoglobulin (IgY), a readily accessible protein derived from eggs, undergoes structural and functional changes upon binding with catechin, which is crucial for expanding its potential uses. This study aims to explore the binding mechanisms, structural alterations, stability changes, and antibacterial properties of the IgY-catechin complex. Using molecular simulation technology, spectroscopy, and antibacterial assays, we investigated the complex in detail. Molecular simulations revealed that catechin binds to key residues (PHE503, THR501, THR505, and GLU511) of IgY, resulting in conformational changes. The predicted free energy of binding was − 27.34 kJ/mol, primarily driven by hydrogen bonding interactions, with a corresponding binding constant of 1.694 × 104 L/mol at 298 K. Circular dichroism (CD) analysis a 5.48% decrease in α-helix content, and an increase in random coil content, reflecting structural changes. Moreover, the IgY-catechin complex demonstrated enhanced acid–base stability but slightly reduced thermal stability compared to IgY alone. Fluorescence microscopy and nucleic acid leakage assays confirmed that the complex disrupted the membranes of Escherichia coli and Staphylococcus aureus, leading to the leakage of intracellular genetic material. These findings reveal that the IgY-catechin interaction not only alters the protein structure of IgY but also boosts its antibacterial activity, offering a promising approach to broaden applications in the food industry.