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Quantitation of the immunodominant 33-mer peptide from α-gliadin in wheat flours

by luciano

In wheat there are multiple fractions able to activate the adverse response of the human immune system. Among these fractions the most active is that called 33-mer because it is the most resistant to human digestion and because it contains six copies of the three toxic epitopes and its intermolecular bonds are very strong. It is therefore important to know the quantity of this fraction in the grains. The study of which some parts are reported, examined 57 different types of wheat, ancient and modern, noting that the difference, in all soft wheat and spelt flour, of 33-mer is wide: from 90.9 to 602.6 μg / g made with flour. On the other hand, its presence in monococcum wheat and durum wheat was not detected. These results take on great importance because they allow grains to be chosen with limited or no presence of this important toxic fraction for products that are more suitable for non-celiac gluten sensitive people or those suffering from gluten disorders.

“All gluten protein fractions, namely the alcohol-soluble prolamins and the insoluble glutelins, contain CD-active epitopes3. The prolamin fraction is particularly rich in proline and glutamine and the numerous proline residues lead to a high resistance to complete proteolytic digestion by human gastric, pancreatic, and brushborder enzymes. Studies by Shan et al. (2002) showed that a large 33-mer peptide (LQLQPFPQPQLPYPQPQLPYPQPQLPYPQPQPF) from α2-gliadin (position in the amino acid sequence of α2-gliadin: 56–88) is resistant to cleavage by intestinal peptidases4,5. The 33-mer is widely called the most immunodominant gluten peptide4,6,7, because it contains three overlapping T-cell epitopes, namely PFPQPQLPY (DQ2.5-glia-α1a, one copy), PYPQPQLPY (DQ2.5-glia-α1b, two copies) and PQPQLPYPQ (DQ2.5-glia-α2, three copies)3, which result in the initiation of a strong immune response.