Gliadin (a type of prolamin) is a class of proteins present in wheat and several other cereals within the grass genus Triticum. Gliadins, which are a component of gluten, are essential for giving bread the ability to rise properly during baking. Gliadins and glutenins are the two main components of the gluten fraction of the wheat seed. This gluten is found in products such as wheat flour. Gluten is split about evenly between the gliadins and glutenins, although there are variations found in different sources. Both gliadins and glutenins are not water-soluble, but gliadins are soluble in 70% aqueous ethanol. There are three main types of gliadin (α, γ, and ω), to which the body is intolerant in coeliac (or celiac) disease. Diagnosis of this disease has recently been improving. Gliadin can cross the intestinal epithelium. Breast milk of healthy human mothers who eat gluten-containing foods presents high levels of non-degraded gliadin. Types The α, γ, and ω gliadin types are separated and distinguished based on their amino acid sequences in the N-terminal cysteine domain. α-/β-gliadins – soluble in low-percentage alcohols. γ-gliadins – ancestral form of cysteine-rich gliadin with only intrachain disulfide bridges ω-gliadins – soluble in higher percentages, 30–50% acidic acetonitrile. Chemistry The gliadins are intrinsically disordered proteins meaning that they have continuously altering shapes making it difficult to study them. The performed image analysis and computer simulations of the proteins show that the average shape of the gliadins follows an elliptical shape. More specifically does the protein likely have a tad-pole like structure with a hydrophobic core and a loose disordered tail. 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. Especially the low molecular weight glutenins are similar in the way that they have cysteines located in matching locations as many of the gliadins. However, the gliadins are unable to form polymers in the cell since its cysteines form intra-chain disulphide bonds at synthesis due to hydrophobic interactions. Gliadins are capable to aggregate into larger oligomers and interact with other gluten proteins, due to large hydrophobic sections, poly-Q and repetative sequences. These sections are likely to aggregate hydrophobicaly, liquid-liquid phase separate, potentially form β-sheets aggregates or simply entagles by its structural properties. Biochemistry Gliadins are prolamins and are separated on the