Ranking of immunodominant epitopes in celiac disease: Identification of reliable parameters for the safety assessment of innovative food proteins.

A ranking of gluten T-cell epitopes triggering celiac disease (CD) for its potential application in the safety assessment of innovative food proteins is developed. This ranking takes into account clinical relevance and information derived from key steps involved in the CD pathogenic pathway: enzymatic digestion, epitope binding to HLA-DQ receptors of the antigen-presenting cells and activation of pro-inflammatory CD4 T-cells, which recognizes the HLA-DQ-epitope complex and initiates the inflammatory response. In silico chymotrypsin digestion was the most discriminatory tool for the ranking of gluten T-cell epitopes among all digestive enzymes studied, classifying 81% and 60% of epitopes binding HLA-DQ2.5 and HLA-DQ8 molecules, respectively, with a high risk. A positive relationship between the number of prolines and the risk of gluten T-cell epitopes was identified. HLA-binding data analysis revealed the additional role played by the flanking regions of the 9-mer epitopes whereas the integration of T-cell activation data into the ranking strategy was incomplete because it was difficult to combine results from different studies. The overall ranking proposed in decreasing order of immunological relevance was: α-gliadins > ω-gliadins > hordeins > γ-gliadins âˆ¼ avenins âˆ¼ secalins > glutenins. This novel approach can be considered as a first step to reshape the risk assessment strategy of innovative proteins and their potential to trigger CD.

In vitro digestion nullified the differences triggered by roasting in phenolic composition and α-glucosidase inhibitory capacity of coffee.

Coffee beans were roasted to medium, dark and very dark degrees, and respective brews were in vitro digested and tested for α-glucosidase inhibition, to explore their antidiabetic potential. Phenolic acids (PA) and Maillard reaction indices (MRI) were quantified before and after digestion. Molecular docking was carried out to investigate α-glucosidase inhibition mechanisms. In vitro digested coffee inhibited α-glucosidase more effectively, compared to undigested samples, but without differences between roasting degrees. The inhibitory effect may be attributed to chlorogenic acids (CGA), which were the most abundant PA in digested coffees. In fact, molecular docking predicted a high affinity of CGA for α-glucosidase. Even though digestion nullified roasting-induced differences in α-glucosidase inhibition, CGA showed a decreasing trend upon digestion. Similarly, MRI did not differ among coffees upon digestion but decreased compared to undigested samples. Overall, the results reported in this study suggest that the presence of different compounds in coffee matrix may contribute to an antidiabetic effect.