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A multi-spectroscopic study on the interaction of food polyphenols with a bioactive gluten peptide: From chemistry to biological implications

Dias, Ricardo, Brás, Natércia F., Pérez-Gregorio, Maria, Fernandes, Iva, Mateus, Nuno, Freitas, Victor
Food chemistry 2019 v.299 pp. 125051
catechin, celiac disease, chemistry, epigallocatechin gallate, epithelium, gluten, intestines, leucine, peptides, phenylalanine, procyanidins, spectroscopy, tyrosine
This study aims to exploit the molecular and cellular mechanisms concerning the functionality of dietary polyphenols (catechin, procyanidin B3, procyanidin C2, epigallocatechin and epigallocatechin gallate) in a nutritional context to prevent Celiac Disease (CD). In that sense, the interaction between the main CD bioactive peptide (32-mer peptide) and some polyphenols was fully characterized at the intestinal level under near physiological conditions by means of different spectroscopic techniques and dynamic simulations. Accordingly, it is proposed that the primarily polyphenol-binding sites on the 32-mer peptide correspond to leucine, tyrosine and phenylalanine containing domains being this interaction entropy-driven. Although procyanidin B3 and trimer C2 had a similar low-affinity constant at 310 K, both procyanidins were able to reduce the 32-mer peptide apical-to-basolateral translocation in in vitro simulated intestinal epithelial barrier thus prospecting the occurrence of additional and still unexplored regulatory mechanisms by which dietary polyphenols might modulate the transepithelial transport of CD bioactive peptides.