Paracellular diffusion mechanism of the egg white-derived peptide RVPSL mediated by tight junction-related protein

This study investigated the paracellular diffusion of egg white-derived antihypertensive peptide RVPSL using a 4D-DIA proteomics approach. The 775 differentially expressed proteins were identified after RVPSL transport. Gene Ontology enrichment analysis indicated that five key proteins (i.e., CLDN1, ECT2, EGFR, SYNPO, and ACTN4) associated with bicellular tight junction assembly, actin filament binding, and actin binding may affect the paracellular diffusion of RVPSL. The egg white-derived peptide RVPSL may trigger the opening of tight junctions by down-regulating the expression of CLDN1 and ECT2 proteins, up-regulating the EGFR protein expression, and may promote the restoration of tight junctions by up-regulating the expression of SYNPO and ACTN4 proteins, thereby enabling paracellular diffusion. Furthermore, the retrograde endocannabinoid signaling pathway may regulate the paracellular diffusion of egg white-derived peptide RVPSL by affecting the expression of tight junction-related proteins. The study provides new ideas and insights to understand the intestinal absorption of egg white-derived peptides to enhance the health-promoting effect.