Intestinal “leak”–Separation of the tight junctions between intestinal cells is the first step in allowing foreign proteins and other fragments access into the bloodstream. This is how autoimmune conditions begin. It allows gliadin itself, gliadin fragments, wheat germ agglutinin and other lectins, bacterial lipopolysaccharide, and other bacterial components to enter the bloodstream. This is why wheat, rye, barley and corn are associated with type 1 diabetes, Hashimoto’s thyroiditism, and rheumatoid arthritis.

Molecular mimicry–In an odd twist of nature, the gliadin protein overlaps in amino acid structure with a number of human proteins, such as transglutaminase, synapsin, and endomysium: molecular mimicry. Should gliadin activate an immune response, the immune response of T and B lymphocytes, antibodies, and other inflammatory mediators will now be misdirected towards an organ of the body–autoimmunity.

Mind effects–While intact gliadin molecules activate intestinal leak and molecular mimicry, gliadin can also be partially digested to peptide fragments, many of them 4- or 5-amino acids long. The unique amino acid sequences of these peptides allow them to act as opiates on the human brain. As opiates (more properly “opioids”), they activate hunger, increase calorie intake, create mental “fog,” and trigger a number of other effects that vary with individual susceptibility: anxiety, anger, food obsessions, repetitive behavior, paranoia, mania, deterioration of attention span, and impulsive behavior.

Intestinal disruption–The unique amino acid structure of gliadin-derived peptides also make them direct bowel toxins that compound the toxicity of another wheat/rye/barley/rice protein called wheat germ agglutinin. Interleukin-mediated inflammation is best documented here.

Allergies–While the various forms of gliadin have always posed potential allergic risks to humans, recent changes in the amino acid structure of gliadin introduced by agribusiness and geneticists have increased allergic potential, especially in the omega-gliadin (one of three classes of gliadin proteins).

Increased celiac disease potential–There is a 33-amino acid long sequence within gliadin that is most powerfully associated with triggering celiac disease. One gene, in particular, coding for this amino acid sequence, Glia-alpha9, was uncommon in the wheat of 1950, but is common in modern semidwarf strains of wheat, explaining why there has been a 400% increase in celiac disease over the last 50 years.