抗氧化剂
丙氨酸
肽
化学
细胞毒性
苯丙氨酸
氨基酸
酪氨酸
亮氨酸
生物化学
肽序列
体外
基因
作者
Yunhui Cheng,Boqun Liu,Bo Cui,Li Wen,Zhou Xu,Mao-Long Chen,Hao Wu
出处
期刊:Nutrients
[MDPI AG]
日期:2023-05-18
卷期号:15 (10): 2373-2373
摘要
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.
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