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<p>Selenium-chelating peptides are a promising class of selenium supplements characterized by favorable absorbability, high bioavailability, and low toxicity. However, the binding mechanism of the current chelation process remains unclear, which also affects the yield of selenium-chelating peptides. In this study, quinoa peptide-selenium chelate (QPI-Se) was prepared and its antioxidant activity reached more than 70%, with high stability at 25℃–45℃ and pH 3–7. A combination of ultraviolet spectroscopy, Fourier transform infrared (FTIR) spectroscopy and scanning electron microscopy (SEM) revealed the emergence of a new substance, namely, selenium-chelating peptide, with absorption peak at 207&#xa0;nm, and symmetric stretching vibrations at 3207.68&#xa0;cm⁻¹ and 1644.56&#xa0;cm⁻¹. Amino acid composition analysis indicated that Leu, Glu, Val, and Asp were the major amino acids involved in the chelation process. Molecular docking model verified that sodium selenite mainly bound to Thr, Leu, Phe, Lys and Val of quinoa peptides, and the major binding sites were identified as amino nitrogen atoms, hydroxyl oxygen atoms, carbonyl oxygen atoms and carboxyl oxygen atoms. This study provides a reference for the chelation mechanism of selenium chelates, and indicates that QPI-Se has the potential to be used as a novel and effective selenium supplement.</p>

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Isolation, identification, and chelation mechanism of selenium-chelating peptides from quinoa protein hydrolysate

  • 期刊论文

  • 发表日期：

    2026年3月26日

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  • Kang Chai,
  • Bin Zhuge,
  • Hong Zong

摘要

Selenium-chelating peptides are a promising class of selenium supplements characterized by favorable absorbability, high bioavailability, and low toxicity. However, the binding mechanism of the current chelation process remains unclear, which also affects the yield of selenium-chelating peptides. In this study, quinoa peptide-selenium chelate (QPI-Se) was prepared and its antioxidant activity reached more than 70%, with high stability at 25℃–45℃ and pH 3–7. A combination of ultraviolet spectroscopy, Fourier transform infrared (FTIR) spectroscopy and scanning electron microscopy (SEM) revealed the emergence of a new substance, namely, selenium-chelating peptide, with absorption peak at 207 nm, and symmetric stretching vibrations at 3207.68 cm⁻¹ and 1644.56 cm⁻¹. Amino acid composition analysis indicated that Leu, Glu, Val, and Asp were the major amino acids involved in the chelation process. Molecular docking model verified that sodium selenite mainly bound to Thr, Leu, Phe, Lys and Val of quinoa peptides, and the major binding sites were identified as amino nitrogen atoms, hydroxyl oxygen atoms, carbonyl oxygen atoms and carboxyl oxygen atoms. This study provides a reference for the chelation mechanism of selenium chelates, and indicates that QPI-Se has the potential to be used as a novel and effective selenium supplement.