School of Food Science and Engineering, Qilu University of Technology (Shandong Academy of Sciences), Jinan 250353, China.
School of Food Science and Bioengineering, Changsha University of Science & Technology, Changsha 410114, China.
Nutrients. 2023 May 18;15(10):2373. doi: 10.3390/nu15102373.
The relationship between the structure of peptides LR5 (LHKFR) and YR6 (YGLYPR) and their antioxidant and anti-inflammatory activity remains unclear. Herein, leucine, tyrosine, proline, and phenylalanine at different positions in the peptides were replaced by Alanine (Ala), and two new pentapeptides (AR5 and LAR5) and four hexapeptides (AGR6, YAR6, YLR6, and YGR6) were obtained. The effect of Ala replacement on the hydrophobicity, cytotoxicity, NO inhibition rate, and active oxygen radical scavenging ability of these peptides and their antioxidant and anti-inflammatory abilities were investigated. The results indicated that the hydrophobicity of the peptides was associated with their amino acid composition and their specific sequence. However, hydrophobicity had no significant effect on cytotoxicity. Ala replacement was shown to enhance hydrophobicity and consequently increased the antioxidant and anti-inflammatory activity of the peptides. The molecular docking studies indicated that the amino acid interactions of the peptide with the Keap1 protein influenced the hydrophobicity and thus affected the antioxidant activity of the peptide.
LR5（LHKFR）和 YR6（YGLYPR）肽的结构与其抗氧化和抗炎活性之间的关系尚不清楚。在此，用丙氨酸（Ala）替换了肽中不同位置的亮氨酸、酪氨酸、脯氨酸和苯丙氨酸，得到了两种新的五肽（AR5 和 LAR5）和四种六肽（AGR6、YAR6、YLR6 和 YGR6）。研究了 Ala 取代对这些肽的疏水性、细胞毒性、NO 抑制率、活性氧自由基清除能力以及抗氧化和抗炎能力的影响。结果表明，肽的疏水性与其氨基酸组成及其特定序列有关。然而，疏水性对细胞毒性没有显著影响。Ala 取代增加了疏水性，从而提高了肽的抗氧化和抗炎活性。分子对接研究表明，肽与 Keap1 蛋白的氨基酸相互作用影响疏水性，从而影响肽的抗氧化活性。
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