The aim of this research is to determine how phenolic acids affect the individual structure of gluten proteins: gliadins and glutenins, by understanding the underlying molecular interactions. Fourier transform infrared spectroscopy was used to determine changes in the secondary structure of the individual gluten network proteins: gliadins and glutenins, after addition of selected phenolic acids to the model dough. Phenolic acids were added to the model dough at the following concentrations: 0.05, 0.1 and 0.2% (w/w). The phenolic acids induce changes in the secondary structure of the gliadins and glutenins. The degree of interaction depends on the structure and concentration of the added phenolic acid. In most cases, these interactions lead to the formation of disordered structures in both gliadins and glutenins. From the results obtained, it can be concluded that the inclusion of certain phenolic acids in the dough affects the hydrogen bonding in gliadins and glutenin, and that phenolic acids interact non-covalently with these gluten proteins. The findings could potentially be applied to food chemistry and may have an impact on the allergenic properties of gluten, particularly in relation to the reduction of the β-turn content within glutenins.Ke y w o r d s: FT-IR spectroscopy, gliadin, phenolic acids, secondary structure, glutenin