Hydrolysis and Transport of Egg White-Derived Peptides in Caco-2 Cell Monolayers and Everted Rat Sacs.

The objective of this paper was to investigate the hydrolysis and transepithelial transport of egg white peptides in Caco-2 cell monolayers and everted rat sacs. Results showed that egg white peptides had higher permeability but lower degradation in Caco-2 cell monolayers than found for everted rat sacs. Peptides LGAKDSTRT, DGSRQPVDN, VNDLQGKTS, and GKKDPVLKD were identified from not only the basolateral (BL) side of Caco-2 cell monolayers but also the serous side of everted rat sacs, suggesting that these four peptides could be transported intact in both model systems. In addition, there were 24 peptides identified from the apical (AP) side of Caco-2 cell monolayers and the mucosal side of everted rat sacs, indicating potential resistance to hydrolysis by brush border membrane peptidases. Among these, peptides IRDLLER, YAEERYP, and IRNVLQPS were demonstrated as having dipeptidyl peptidase IV (DPP-IV) inhibitory activities with IC50 values of 186.23 ± 15.25, 340.62 ± 4.73, and 598.28 ± 15.12 μM ( P < 0.05), respectively. Furthermore, molecular docking revealed that the DPP-IV inhibitory peptides were predicted to form hydrogen-bonds, π-π bonds, and charge interactions with the activity sites, especially the amino acid residues located in the S2 pocket of DPP-IV, potentially contributing to their DPP-IV inhibitory activities.