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Structurally manipulated antioxidant peptides derived from wheat bran: Preparation and identification

[Display omitted] •91 bioactive peptides were identified from wheat bran (WB) by virtual screening.•WB peptides were rich in hydrophobic amino acids, leading to excellent bioactivity.•WB peptides showed high antioxidant activity against oxidative damage in HepG2 cells.•DLDW and DLGL with the highest...

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Bibliographic Details
Published in:Food chemistry 2024-06, Vol.442, p.138465-138465, Article 138465
Main Authors: Zhuang, Min, Li, Jiaqing, Wang, Anqi, Li, Gaoheng, Ke, Sheng, Wang, Xuanyu, Ning, Ming, Sheng, Zhanwu, Wang, Bing, Zhou, Zhongkai
Format: Article
Language:English
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Summary:[Display omitted] •91 bioactive peptides were identified from wheat bran (WB) by virtual screening.•WB peptides were rich in hydrophobic amino acids, leading to excellent bioactivity.•WB peptides showed high antioxidant activity against oxidative damage in HepG2 cells.•DLDW and DLGL with the highest binding capacity were promising Keap1-Nrf2 inhibitors. Bioactive peptide’s development is facing two challenges in terms of its lower yield and limited understanding of structurally orientated functionality. Therefore, peptides were prepared from wheat bran via a cocktail enzyme for achieving a higher level of hydrophobic amino acids than traditional method. The obtained peptides exhibited great antioxidant activities against H2O2-induced oxidative stress in HepG2 cells. Among them, 91 bioactive peptides were selected through the virtual screening, and their N-terminal and C-terminal contained many hydrophobic amino acids. Then the peptides with capacity to interact with Keap1 were identified by in silico simulation, because Keap1 acts as a sensor of redox insults. The results revealed that peptides DLDW and DLGL demonstrated the highest binding affinities, and a bridge was formed between Asp of DLGL and Arg415 of Klech domain, contributing to interfering Keap1-Nrf2 interaction. These findings implied a potential application of wheat bran peptides as nutraceuticals and health-promoting ingredients.
ISSN:0308-8146
1873-7072
DOI:10.1016/j.foodchem.2024.138465