Kinetic dependencies reveal unique adsorption behaviors in recombinant pea vicilin and cupin-1.2 proteins in 8M urea, suggesting complex layer structures.
The kinetic dependencies of the surface pressure, the dilational dynamic surface elasticity and ellipsometric angles of cupin-1.2 and vicilin solutions in 8M urea were measured at different concentrations. The analysis of these kinetics dependencies and the obtained master curves allowed us to determine a few adsorption steps in the investigated systems and showed that the master curves are individual characteristics of the protein for a given solvent. At the same time, the shape of these curves can be different for adsorbed and spread layers of plant proteins indicating different structures of these layers. The dependencies of the dynamic surface elasticity on surface pressure are non-monotonic, unlike the corresponding results for most of the solutions of the investigated plant proteins. The extremums of these dependencies can be connected to the formation of the distal region of the surface layer in agreement with the theory for the surface viscoelasticity of polymer solutions.
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Isakov et al. (2025) studied this question.
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