HYDROPHOBIC INTERACTIONS BETWEEN GLIADIN AND PROTEINS AND CELIAC-DISEASE

Gliadin-protein interaction and its relationship to the pathogenesis h ypotheses of celiac disease was investigated. Wheat germ agglutinin wa s not immunodetected in gliadin preparations. Peptic-tryptic gliadin d igest was used to study the gliadin-protein interactions by crossed im munoelectrophoresis and affinity blotting. Biotinylated gliadin digest interacted with IgG and bovine serum albumin but not with several gly coproteins. Since albumin and IgG light chains are not glycosylated, t his interaction is not lectin-like, neither completely immunological b ecause of recognition of the IgG Fc fraction. Immobilized and boiled I gG was not recognized by gliadin digest as a lectin. Gliadin digest fr actions from T-gel chromatography reduced the fluorescence intensity o f cis-parinaric acid bound to albumin. The gliadin-protein interaction is not lectin-like or completely immunological but hydrophobic. Hydro phobicity of gliadins may contribute to the pathogenic events that res ult in celiac disease.