Hydrolysis and transepithelial transport of two corn gluten derived bioactive peptides in human Caco-2 cell monolayers.

The objective of this paper was to investigate the transepithelial transport of two novel corn gluten-derived antioxidant peptides, YFCLT and GLLLPH, using Caco-2 cell monolayers. Results showed that both of YFCLT and GLLLPH could transport in intact form across Caco-2 cell monolayers with apparent permeability coefficient (Papp ) values of (1.10±0.16)×10-7 cm/s and (1.98±0.23)×10-7 cm/s, respectively. However, it was found that the two peptides were susceptible and easily hydrolyzed by brush border membrane peptidases. In the presence of diprotin A, an inhibitor of dipeptidyl peptidase IV (DPPIV), the hydrolysis of YFCLT and GLLLPH decreased and their permeabilities increased significantly compared to control group (P<0.05). The results of transport routes revealed that Gly-Sar, a peptide transporter 1 (PepT1) substrate, had little effects on the transepithelial permeability (P>0.05), suggesting that the transport of YFCLT and GLLLPH across Caco-2 cell monolayers was not mediated by PepT1. However, it was found that cytochalasin d, a tight junctions (TJs) disruptor, increased the permeability significantly (P<0.05). While wortmannin, a transcytosis inhibitor, and sodium azide, an ATP synthesis inhibitor, both decreased the permeability significantly (P<0.05). It indicated that the TJs-mediated paracellular pathway and energy-dependent transcytosis were involved in the transport of YFCLT and GLLLPH across Caco-2 cell monolayers.