Soybean meal peptide Gly-Thr-Tyr-Trp could protect mice from acute alcoholic liver damage: A study of protein-protein interaction and proteomic analysis.

Alcoholic liver disease (ALD) is a serious health threat. Soybean meal peptide (SMP) supplementation may protect against this damage; however, the potential mechanism underlying the specific sequence of SMPs is unclear. Protein-protein interaction and proteomic analyses are effective methods for studying functional ingredients in diseases. This study aimed to investigate the potential mechanism of action of the peptide Gly-Thr-Tyr-Trp (GTYW) on ALD using protein-protein interaction and proteomic analyses. These results demonstrate that GTYW influenced the targets of glutathione metabolism (glutathione-disulfide reductase, glutathione S-transferase pi 1, and glutathione S-transferase mu 2). It also regulated the expression of targets related to energy metabolism and amino acid conversion (trypsin-2, cysteine dioxygenase type-1, and F6SJM7). Amino acid and lipid metabolisms were identified based on Gene Ontology annotation. These results indicate that GTYW might affect alcohol-related liver disease signaling pathways. This study provides evidence of the protective and nutritional benefits of SMPs in ALD treatment.

Transcriptome analysis reveals the hepatoprotective mechanism of soybean meal peptides against alcohol-induced acute liver injury mice.

This study aimed was to explore the hepatoprotective potential of soybean meal peptides (SPs) against alcohol-induced liver injury and investigate the underlying mechanisms through transcriptome analysis. The chemical antioxidant analysis of SPs exhibited potent ABTS radical scavenging capacity (11.94 ± 0.41 mg TE/100 mg peptide), ferric reducing antioxidant power (6.42 ± 0.32 mmol Fe2+/100 mg peptide), and oxygen radical absorption capacity (14.78 ± 0.01 mg TE/100 mg peptide). Moreover, SPs increased cell viability and reduced intracellular reactive oxygen species levels in Caco-2 cells by H2O2-induced, and without cytotoxicity. In the mice model, preintervention with SPs reduced the levels of aspartate transaminase/alanine transaminase, total cholesterol, triglyceride and malondialdehyde by alcohol-induced, meanwhile, increased the levels of total superoxide dismutase, glutathione and catalase by alcohol-induced. Histological analysis showed that SPs alleviated the liver injury by alcohol-induced and no toxic effects on the kidneys. According to transcriptome analysis, 1737 genes were significantly differentially expressed (1076 up-regulated and 661 down-regulated) after SPs pretreatment. The main functions of these genes were related to inflammation, lipid metabolism and oxidation. The findings from the present study suggested that SPs produced positive hepatoprotection and showed potential to be used as a dietary supplement or an ingredient of functional food.

Egg white peptides ameliorate dextran sulfate sodium-induced acute colitis symptoms by inhibiting the production of pro-inflammatory cytokines and modulation of gut microbiota composition.

Egg white peptides (EWPs) can be effectively used to alleviate and treat inflammatory diseases due to their anti-oxidation, anti-inflammation, and microbiota regulation capabilities. A dextran sodium sulfate (DSS)-induced colitis model was used to clarify the regulatory effects of EWPs on colitis. Forty-three peptide sequences were identified from EWPs using LC-MS/MS. The results demonstrated that EWPs decreased the levels of pro-inflammatory cytokines and the extent of crypt damage in a dose-dependent manner. 16S rRNA gene sequencing results indicated that 200 mg/kg EWPs significantly increased the relative abundance of beneficial bacteria Lactobacillus and Candidatus_Saccharimonas, and reduced the relative abundance of pathogenic bacteria Ruminiclostridium and Akkermansia. In addition, the degree of correlation between pro-inflammatory cytokines and microbiota was as follows: interleukin (IL)-1ß > IL-8 > IL-6 > tumor necrosis factor-α To summarize, EWPs contributed to the alleviation of colitis symptoms and the intestinal injury through anti-inflammatory effects, repair of intestinal mucosa, and modulation of gut microbiota.

Soybean Peptide QRPR Activates Autophagy and Attenuates the Inflammatory Response in the RAW264.7 Cell Model.

BACKGROUND: There are few studies on the autophagy and inflammatory effects of soy peptides on the inflammatory cell model. Further insight into the underlying relationship of soybean peptides and autophagy needs to be addressed. Therefore, it is worthwhile investigating the possible mechanisms of soybean peptides, especially autophagy and the inflammatory effects. OBJECTIVE: In this study, we used a RAW264.7 cell inflammation model to study the inhibitory effect and mechanism of soybean peptide QRPR on inflammation. METHODS: We used LPS-induced inflammation model in RAW264.7 cells to study the inhibitory effect and mechanism of soybean peptide QRPR on inflammation. First, Cell viability was determined by cell activity assay. Subsequently, the concentrations of the inflammatory cytokines IL-6 and TNF-α were measured by ELISA. IL-6, TNF-α, Beclin1, LC3, P62, PIK3, AKT, p-AKT, pmTOR and mTOR protein expression were detected by western-blot. PIK3, AKT and mTOR gene expression level were quantified by quantitative real-time PCR. Double-membrane structures of autophagosomes and autolysosomes were observed by transmission electron microscopy. The PI3K/AKT/mTOR signaling pathway in LPS-induced RAW264.7 cells was speculated when the autophagy was activated. RESULTS: The results showed that QRPR activates autophagy in the inflammatory cell model and that the inhibitory effect of QRPR on inflammation is reduced after autophagy was inhibited. Western- blot and real-time PCR results indicated that QRPR activates autophagy in LPS-induced RAW264.7 cells by modulating the PI3K/AKT/mTOR signaling pathway, and it shows a significant time dependence. CONCLUSION: This study indicated that the soybean peptide QRPR activates autophagy and attenuates the inflammatory response in the LPS-induced RAW264.7 cell model.