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Gliadin and related gluten prolamins are a group of alcohol-soluble storage proteins found in wheat, barley, and rye that are characterized by high proline and glutamine content (Source: UniProt). These proteins are resistant to complete digestion by human gastrointestinal proteases, leaving behind large, immunogenic peptides such as the 33-mer fragment (Source: PubMed, PMID: 12364798). In individuals with Celiac disease, these peptides cross the intestinal barrier and trigger an inflammatory immune response mediated by T-cells, leading to villous atrophy and malabsorption (Source: NIH, NIDDK). As a therapeutic target, gliadin is addressed through various strategies including enzymatic degradation by oral proteases like latiglutenase, which cleaves the protein into non-toxic fragments (Source: ClinicalTrials.gov). Other approaches include the use of sequestering polymers to prevent gluten absorption or nanoparticles designed to induce immune tolerance to gliadin antigens (Source: Takeda Pharmaceuticals).
Proteolytic degradation of immunogenic peptides, non-absorbable sequestration, and induction of immune tolerance.
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