Alpha- and beta-gliadins are subfractions of gliadin, a prolamin class protein found in wheat. Biochemically, these peptides are rich in proline and glutamine, which can make certain fragments resistant to complete digestion and more likely to persist as peptide chains that interact with the immune system. Gliadin fractions were characterized as part of historical efforts to define gluten components and their interactions with human immunity. At the peptide level, alpha-beta gliadin fragments are commonly measured in research and clinical labs to map specific antibody responses and to refine understanding of wheat-related immune patterns.

Elevated IgA or IgG antibodies to alpha-beta gliadin suggest that the immune system has mounted a measurable response to wheat-derived peptides. IgA elevations are more consistent with mucosal or gut-associated exposure, while IgG elevations generally reflect broader systemic immune recognition. These patterns can be associated with increased likelihood of food-related immune activity, but interpretation depends on the full Food Zoomer profile and clinical context. Low or undetectable antibody levels indicate no measurable IgA/IgG response to alpha-beta gliadin at the time of testing. Low results may reflect immune tolerance, lack of recent exposure, assay timing, or individual immune variability and should be considered alongside other panel markers and clinical information.

Alpha-Beta Gliadin is included in the Food Zoomer to assess wheat-derived peptide immune activity at the peptide level. By measuring both IgA and IgG to these fragments, the marker helps identify whether wheat-related immune recognition is primarily mucosal or systemic and contributes to pattern-based, personalized dietary planning.