%0 Journal Article
%T Structurally manipulated antioxidant peptides derived from wheat bran: Preparation and identification.
%A Zhuang M
%A Li J
%A Wang A
%A Li G
%A Ke S
%A Wang X
%A Ning M
%A Sheng Z
%A Wang B
%A Zhou Z
%J Food Chem
%V 442
%N 0
%D 2024 Jun 1
%M 38266414
%F 9.231
%R 10.1016/j.foodchem.2024.138465
%X 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.