While protein-stabilized emulsions have demonstrated potential for various applications in food, their poor lipid oxidation remains a major challenge. The relationship between the architecture of polyphenolic compounds and their capacity to suppress lipid oxidation has not received extensive scrutiny. In this research, pea protein isolate (PPI)–polyphenol complexes were synthesized to examine their capability of maintaining emulsion stability and suppressing lipid oxidation. The collective evidence from fluorescence spectroscopy and molecular dynamics simulations pointed towards non-covalent and self-initiated interactions between the polyphenols and PPI. The presence of additional hydroxyl groups on the polyphenols could significantly boost the extent of these interactions. Specific clusters in PPI and polyphenols which might have formed hydrogen bonds and hydrophobic interactions. Polyphenols also reduced the interfacial tension and increased the surface hydrophobicity of the complex, thus driving more proteins to adsorb at the oil–water interface. The PPI-rosmarinic acid (RA)-stabilized emulsion had a smaller droplet size and higher electrostatic repulsion, enabling it to resist droplet aggregation. This emulsion stood out as having the most robust stability amongst all PPI-polyphenol emulsions and proved highly efficient in preventing lipid oxidation. This study bolsters the viability of employing polyphenol and pea protein-stabilized emulsions in developing new food products.

Background: Valtrate (Val) was extracted from the Valeriana jatamansi Jones plant, had good antitumor activity. However, its precise molecular mechanism in cancer cells was still unclear. This study investigated the effect of Val on gastric cancer (GC) cells and its potential molecular mechanism. Methods: Cell viability was examined by CCK-8 assay. Cell cycle, apoptosis, and Reactive oxygen species (ROS) level were analyzed by flow cytometry. The migration effect of Val on AGS cells was analyzed by transwell and wound-healing assay. The expression levels of proteins were analyzed by western blot. Results: The cell viability assay results demonstrated that Val significantly decreased GC cell viability. Apoptosis assay results revealed that Val induced mitochondria-dependent apoptosis through the Bad/Bcl-2/cyto-c/cle-casp-3/cle-PARP pathways. Further exploration found that Val induced apoptosis through increasing the expression of phosphorylated p38 mitogen-activated protein kinase (p-p38), phosphorylated c-Jun N-terminal kinase (p-JNK), and Inhibitor kappa B alpha (IκB-α) proteins and decreasing the expression of phosphorylated extracellular signal-regulated kinase (p-ERK), phosphorylated signal transducer and activator of transcription 3 (p-STAT3), and nuclear factor kappa-B (NF-κB) proteins; these expression levels of proteins were reversed by mitogen-activated protein kinase (MAPK) inhibitor. Furthermore, Val induced G2/M phase arrest in AGS cells through downregulating the expression of phosphorylated protein kinase B (p-AKT). Moreover, Val induced inhibition of AGS cell migration through downregulating the expression of p-GSK-3β and β-catenin. In addition, Val promoted the ROS accumulation of AGS cells. Further investigation found that Val-induced apoptosis, arrested the cell cycle, and inhibited cell migration, and that its signaling pathways related to protein expressions were reversed by the ROS scavenger, N-acetyl-L-cysteine. Conclusion: Val induced apoptosis, arrested the cell cycle, and inhibited migration by ROS-mediated MAPK/STAT3/NF-κB, AKT/Cyclin B/CDK1/2, and GSK-3β/β-catenin signaling pathways in AGS cells.