Gliadin

Breast milk of healthy human mothers who eat gluten-containing foods presents high levels of non-degraded gliadin.

[2][3] The α, γ, and ω gliadin types are separated and distinguished based on their amino acid sequences in the N-terminal cysteine domain.

[4][5] The gliadins are intrinsically disordered proteins meaning that they have continuously altering shapes making it difficult to study them.

[8] Compared to the other gluten proteins like the glutenins, which form extended networks of polymers due to disulphide bonds, gliadins are monomeric molecules in the cell, even if they in many ways are very similar.

Gliadins are capable to aggregate into larger oligomers and interact with other gluten proteins, due to large hydrophobic sections, poly-Q and repetitive sequences.

Gliadin proteins have the ability to provoke an autoimmune enteropathy (intestinal disease) caused by an abnormal immune response in genetically susceptible individuals.

[14] Celiac disease with "non-classic symptoms" is the most common clinical type and occurs in older children (over 2 years old), adolescents and adults.

[19] It is characterized by milder or even absent gastrointestinal symptoms and a wide spectrum of non-intestinal manifestations that can involve any organ of the body, and very frequently may be completely asymptomatic[17] both in children (at least in 43% of the cases[20]) and adults.

[17] Untreated celiac disease may cause malabsorption, reduced quality of life, iron deficiency, osteoporosis, an increased risk of intestinal lymphomas and greater mortality.