Owing to its extensive use in the human diet, wheat is among the most common causes of food-related
allergies and intolerances.
Allergies to wheat are provoked by ingestion, inhalation or contact with either the soluble or the insoluble
gluten proteins in wheat.
Gluten proteins, and particularly the
gliadin fraction, are also the main factor triggering
celiac disease, a common enteropathy induced by ingestion of wheat
gluten proteins and related
prolamins from oat, rye and barley in genetically susceptible individuals. The role of
gliadin and of its derived
peptides in eliciting the adverse reactions in
celiac disease are still far from being completely explained. Owing to its unique pathogenesis,
celiac disease is widely investigated as a model immunogenetic disorder. The structural characterization of the injuring agents, the
gluten proteins, assumes a particular significance in order to deepen the understanding of the events that trigger this and similar diseases at the molecular level. Recent developments in proteomics have provided an important contribution to the understanding of several basic aspects of wheat
protein-related diseases. These include: the identification of
gluten fractions and derived
peptides involved in
wheat allergy and intolerance, including
celiac disease, and the elucidation of their mechanism of toxicity; the development and validation of sensitive and specific methods for detecting trace amounts of
gluten proteins in
gluten-free foods for intolerant patients; and the formulation of completely new substitute foods and ingredients to replace the
gluten-based ones. In this article, the main aspects of current and prospective applications of mass spectrometry and proteomic technologies to the structural characterization of
gluten proteins and derived
peptides are critically presented, with a focus on issues related to their detection, identification and quantification, which are relevant to the biochemical, immunological and toxicological aspects of wheat intolerance.