Nanomechanical force measurements of gliadin protein interactions

The strength and nature of interactions between monomeric gliadin proteins involving α-α, ω-ω, and α-ω interactions in 0.01 M acetic acid, and the effect of urea has been investigated. It was shown by means of nanomechanical force measurements that the stretching events in the separation curve after adhesive phenomena originated from proteins. These stretching events displayed different responses of the α- and ω-gliadins to urea. While 2M urea caused the more globular α-gliadins to unfold, the β-turn-rich ω-gliadins remained fairly stable even in 8M urea. This suggests different roles for gliadins in the formation of dough; while the ω-gliadins are still in a compact structure being responsible for the viscous flow, the α-gliadins have already started to participate informing the network in dough.