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

  • Food Chem. 2024 Jun 1:442:138465. doi: 10.1016/j.foodchem.2024.138465.
Min Zhuang  1 ,  Jiaqing Li  2 ,  Anqi Wang  1 ,  Gaoheng Li  1 ,  Sheng Ke  1 ,  Xuanyu Wang  1 ,  Ming Ning  3 ,  Zhanwu Sheng  4 ,  Bing Wang  5 ,  Zhongkai Zhou  6
Affiliations
  • 1. College of Food Science and Engineering, Tianjin University of Science and Technology, Tianjin 300457, China.
  • 2. School of Chemical Engineering, University of Chinese Academy of Sciences, Beijing 100049, China.
  • 3. Key Laboratory for Processing and Quality Safety Control of Characteristic Agricultural Products, the Ministry of Agriculture and Rural Affairs, Shihezi University, Shihezi 832003, China.
  • 4. Haikou Experimental Station, Chinese Academy of Tropical Agricultural Sciences, Haikou 570101, China.
  • 5. Gulbali Institute-Agriculture Water Environment, Charles Sturt University, Wagga Wagga, NSW 2678, Australia.
  • 6. College of Food Science and Engineering, Tianjin University of Science and Technology, Tianjin 300457, China; Key Laboratory for Processing and Quality Safety Control of Characteristic Agricultural Products, the Ministry of Agriculture and Rural Affairs, Shihezi University, Shihezi 832003, China; Gulbali Institute-Agriculture Water Environment, Charles Sturt University, Wagga Wagga, NSW 2678, Australia. Electronic address: [email protected].
PMID: 38266414 DOI: 10.1016/j.foodchem.2024.138465
Abstract

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.

Keywords
Antioxidant activity; Bioactive peptides; Cellular model; Keap1-Nrf2 interaction; Molecular docking; Wheat Bran.
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