Protective effect of vitexin against high fat-induced vascular endothelial inflammation through inhibiting trimethylamine N-oxide-mediated RNA m6A modification.

A high-fat diet (HFD) is a major risk factor for cardiovascular disease. However, the specific effects of a HFD on vascular inflammation and the protective role of vitexin, a bioactive compound derived from food, require further research. This study investigated the protective effects of vitexin intervention against HFD-induced vascular inflammation and its underlying mechanism. The results demonstrated that vitexin intervention significantly reduced body weight, serum total cholesterol, and low-density lipoprotein cholesterol levels in HFD-fed mice. Vitexin also improved vascular pathological changes and the inflammatory status in the mice. Furthermore, vitexin intervention reduced serum TMAO levels in HFD-fed mice by altering the gut microbiota composition. The HFD significantly increased N6-methyladenosine (m6A) levels in aorta tissues, while vitexin intervention reversed this abnormal m6A level. Through metabolite affinity responsive target fluorescence quenching and molecular docking assays, it was found that vitexin could directly bind to fat mass and obesity-associated protein (FTO), potentially promoting m6A demethylation. The dose-response relationship between TMAO and inflammation/m6A was further validated in HUVEC cells and in vivo mouse experiments. Specifically, TMAO increased m6A levels and inflammation, while vitexin inhibited TMAO-mediated m6A modification, exhibiting anti-inflammatory effects. In conclusion, this study demonstrates the protective role of vitexin against HFD-induced vascular inflammation by inhibiting TMAO-mediated RNA m6A modification, laying the foundation for the development of functional foods.

Comparative Analysis of Protein Digestion Characteristics in Human, Cow, Goat, Sheep, Mare, and Camel Milk under Simulated Infant Condition.

An infant in vitro digestion model was utilized to investigate protein digestion characteristics in human and diverse mammalian milk (i.e., cow, goat, sheep, mare, and camel milk) using electrophoresis and chromatography. Digestive differences among milks were mainly manifested in the infant gastric phase, as evidenced by varying degrees of protein digestion. Notably, proteins (i.e., lactoferrin, serum albumin, and immunoglobulin G-heavy chain) remained partially intact in human milk, whereas these proteins in animal milk were exclusively degraded after gastrointestinal digestion. The peptide spectra of human, mare, and camel milk were highly similar, with a predominant formation of low-intensity small peptides, whereas the other three milk showed the opposite phenomenon. Heatmap cluster analysis indicated that camel milk was the most comparable to human milk before digestion, yet sheep milk was the most similar to human milk regarding protein digestion behaviors following infant gastric digestion.

Nutritional composition and proteomic analysis of soft-shelled turtle (Pelodiscus sinensis) egg and identification of oligopeptides with alpha-glucosidase inhibitory activity.

This study aimed to explore nutritional compositions and proteomics of soft-shelled turtle (SST) egg, as well as identify potential antidiabetic oligopeptides with α-glucosidase inhibitory property. Results revealed that SST egg is a promising source of highly nutritious proteins and minerals (54.64% and 5.81% of dry matter, respectively). Further proteomic analysis showed SST egg proteins contained at least 9 protein families, such as transferrin/iron binding protein and immunoregulation-related protein. Hydrolysis by different enzymes, especially papain, remarkably increased α-glucosidase inhibitory activity and scavenging activity for ABTS, DPPH, hydroxyl and oxygen radicals of SST egg proteins. Peptides from papain hydrolysate were fractionated using ultrafiltration followed by reverse phase chromatography, and 16 peptides were identified in the most active fraction by LC-QTOF-MS/MS. Molecular docking revealed that 14 of these peptides could easily dock into the substrate-binding pocket and/or inhibitor binding sites of α-glucosidase with the docking score below -150 kcal/mol, indicating their potential α-glucosidase inhibitory properties. The five most abundant oligopeptides with potent interaction with α-glucosidase were further synthesized, and oligopeptides HNKPEVEVR, ARDASVLK and SGTLLHK strongly inhibited the activity of α-glucosidase (IC50 of 56, 195 and 289 µmol/L, respectively). Therefore, oligopeptides from enzymatic hydrolysate of SST egg protein exhibit potential antidiabetic activity, making it a promising functional food ingredient.