glutenbinding

Glutenbinding refers to the set of molecular interactions by which gluten proteins engage with other molecules, with significance in both food science and biology. It is not a single receptor or pathway, but a collection of binding events that shape gluten’s properties in dough and its interactions with the human immune system in susceptible individuals.

In food science, gluten consists mainly of gliadins and glutenins. Their interactions occur through hydrophobic contacts, hydrogen bonding, ionic interactions, and disulfide cross-links among glutenin subunits. These bindings form a viscoelastic network that contributes to dough strength, extensibility, and gas retention, while binding to starch and other components influences dough texture. Processing conditions such as mixing, hydration, and temperature modulate these interactions.

In the context of celiac disease and gluten sensitivity, certain gluten-derived peptides bind to the intestinal mucosa. Tissue transglutaminase 2 deamidates specific glutamine residues, increasing the negative charge and affinity of these peptides for HLA-DQ2 or HLA-DQ8 molecules on antigen-presenting cells, which can promote an inflammatory T-cell response in genetically predisposed individuals. Thus, gluten binding in this context relates to peptide–receptor and peptide–HLA interactions that contribute to immunogenicity.

Research on glutenbinding also includes methods to study these interactions, such as binding assays, affinity chromatography, and surface plasmon resonance. It encompasses the development of gluten-binding agents or binders intended to reduce gluten exposure or mitigate gluten-related disorders, though such approaches are investigational and subject to regulatory evaluation.