Abstract
Trp, Phe, and Tyr ethyl esters and their dipeptides with Gly at the C-terminals inhibited ovalbumin (OVA) permeation through Caco-2 monolayers. The inhibitory activity of Trp ethyl ester was the highest at near the concentration of 10-6 M. It was suggested that Trp ethyl ester inhibited transcellular permeation of OVA.