Dynamic properties of the layers of cupin-1.1 aggregates at the air/water interface

Spread layers of amorphous aggregates of the structural domain of plant protein vicilin, cupin-1.1, at the water – air interface were studied by the surface tensiometry, dilational surface rheology, Brewster angle and atomic force microscopy. The layer properties differed strongly from the results for the layers of previously studied proteins. The dependency of the dynamic elasticity of the layer on surface pressure had two local maxima with the second peak being four times higher than the first one. In the region of the first maximum the obtained results are similar to those for dispersions of polymer microgels with a hairy corona. At the beginning of surface compression separate threads of the corona are stretched along the surface and the surface elasticity increases. The further compression results in the formation of loops and tails leading to a decrease of the elasticity. The second local maximum of the dynamic surface elasticity is presumably caused by the interactions of the rigid cores of the aggregates leading finally to the formation of multilayer structures at high surface pressures. In this case, the surface elasticity starts to decrease as a result of the segment exchange between different layers at the interface. [Display omitted] •Morphology of cupin-1.1 aggregate layers depends on urea concentration in subphase.•Surface elasticity of cupin-1.1 aggregate layers has two maxima.•Surface elasticity of these layers is determined by cupin-1.1 aggregate structure.•Surface elasticity peaks depend on the degree of protein unfolding.