Antarctic Krill Derived Nonapeptide as an Effective Iron-Binding Ligand for Facilitating Iron Absorption via the Small Intestine

Abstract

) iron-binding peptides was used in this study to analyze its iron-binding sites and structural changes after iron coordination. The enzymatic resistance and transport of DTDSEEEIR-iron during gastrointestinal digestion and absorption as well as the relationship between the DTDSEEEIR stability and the enhancement of iron absorption were further explored. Results revealed that iron ions spontaneously bound to the carboxyl, hydroxyl, and amino groups of the DTDSEEEIR peptide, which induced the folding of DTDSEEEIR to form a more orderly structure. The DTDSEEEIR peptide remained stable to a certain extent (79.60 ± 0.19%) after gastrointestinal digestion and the coordination of iron improved the digestive stability of the DTDSEEEIR peptide (93.89 ± 1.37%). Moreover, the stability of DTDSEEEIR across intestinal epithelium had a positive effect on iron absorption, which implied that DTDSEEEIR might carry iron ions through intestinal epithelial cells.