Shipin gongye ke-ji (Aug 2024)

Screening of Anti-hyperuricemia Peptides from Oat Protein Based on High-throughput Transcriptome Sequencing and Network Pharmacology

  • Siting FENG,
  • Pei LIU,
  • Yihe ZHANG,
  • Xianjing WU,
  • Shuqiang REN,
  • Fei GAO

DOI
https://doi.org/10.13386/j.issn1002-0306.2023100096
Journal volume & issue
Vol. 45, no. 15
pp. 10 – 24

Abstract

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Initiating from omics, the research aimed to discover and filter oat active peptides effective against hyperuricemia, and to study the operational mechanism of these oat active peptides in treating hyperuricemia. In the present study, RNA was extracted from oat grains for high-throughput transcriptomic sequencing, and oat grain protein sequences were acquired by comparing with a reference genome and quantifying the expression of protein-coding genes. Active components of oat peptides were selected by employing high-throughput enzymolysis in silico, Peptide Ranker, and ADME/T. Network pharmacology were utilized to discover active peptides from oat proteins that were effective against hyperuricemia. The findings indicated that for 'Bayou No.1' and 'Baiyan No.7' oat grains, the counts of protein sequences expressed with under 90% repeatability during the grain formation and grain-filling phases were respectively 6310, 3157, and 5804, 5107. The optimal peptide library was from the protein sequences of 'Bayou No.1' naked oat in the grain-filling stage, processed through simulated enzymatic digestion in silico with proteinase K, yielding a library with 42 oat active peptides predicted to have potential activity and favorable pharmacological properties. The initial screening revealed key oat active peptides sequences against hyperuricemia to be PPF, PPPL, MPF, MPL, and PPPF, potentially targeting genes like ALB, IL1B, SRC, CASP3, and STAT3, influencing pathways in cancer, lipid and atherosclerosis, and chemically induced carcinogenesis-receptor activation to mitigate hyperuricemia. Molecular docking showed that binding energy <-5 kJ/mol accounted for 82.86%, indicating that the main active components of oat peptides had good binding activity with most of the targets. The optimal oat synthetic peptide PPF showed good xanthine oxidase inhibition (IC50=6.132 mmol/L). Naked oat protein can act as a promising precursor for the enzymatic release of active peptides effective against hyperuricemia, and also offers theoretical guidance for producing bioactive peptides through oat protein enzymolysis and developing functional foods using oat active peptides to combat hyperuricemia.

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