Deamidated gliadin peptide (DGP) (DGP)

Deamidated gliadin peptide (DGP) is a modified dietary peptide derived from wheat gluten that acts as the central pathogenic antigen in Celiac disease. In the intestinal lamina propria, the enzyme tissue transglutaminase (tTG or TG2) converts specific glutamine residues in gliadin into glutamic acid, a process known as deamidation (Sollid et al., 2000). This modification creates a negative charge that significantly increases the peptide's affinity for HLA-DQ2 and HLA-DQ8 molecules on antigen-presenting cells, thereby triggering a robust T-cell mediated immune response (Dieterich et al., 1997). This response leads to chronic inflammation, villous atrophy, and the production of diagnostic anti-DGP antibodies. While DGP is not a traditional therapeutic target like a receptor, it is the focal point of several therapeutic strategies, including the use of tTG inhibitors like ZED1227 to prevent its formation and gluten-degrading enzymes like latiglutenase to eliminate its precursors (Schuppan et al., 2021; Syage et al., 2017). Additionally, novel immunotherapies such as TAK-101 utilize gliadin peptides to induce immune tolerance and prevent the inflammatory cascade (Kelly et al., 2021).

Other names

Deaminated gliadin peptideDeamidated gluten peptidetTG-modified gliadinDGP

Prevention of deamidated gliadin peptide formation through tissue transglutaminase inhibition, enzymatic degradation of gluten precursors, or induction of immune tolerance.