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During wheat seeds development, storage proteins are synthetized and subsequently form dense protein phases, also called Protein Bodies (PBs). The mechanisms of PBs formation and the supramolecular assembly of storage proteins in PBs remain unclear. In particular, there is an apparent contradiction between the low solubility in water of storage proteins and their high local dynamics in dense PBs. Here, we probe the interplay between short-range attraction and long-range repulsion of a wheat gliadin isolate by investigating the dynamics of liquid-liquid phase separation after temperature quench. We do so using time-resolved small angle light scattering, phase contrast microscopy and rheology. We show that gliadins undergo liquid-liquid phase separation through Nucleation and Growth or Spinodal Decomposition depending on the quench depth. They assemble into dense phases but remain in a liquid-like state over an extended range of temperatures and concentrations. The analysis of phase separation kinetics reveals that the attraction strength of gliadins is in the same order of magnitude as other proteins. We discuss the respective role of competing interactions, protein intrinsic disorder, hydration and polydispersity in promoting local dynamics and providing this liquid-like behavior despite attractive forces. ispartof: SCIENTIFIC REPORTS vol:8 issue:1 ispartof: location:England status: published

Phase separation in aqueous biopolymer mixtures results in the formation of an interface, separating two aqueous bulk phases. The properties of that interface are key parameters to understand and predict phenomena, such as the phase-separation process and deformation of droplets in a flow field. In these processes, the structures and sizes of the morphologies depend on the balance between viscous and interfacial forces. Normally, one assumes that the interfacial tension is the only important parameter regarding the interfacial forces. However, we will show that in these water-in-water emulsions, bending rigidity and interfacial permeability also play an important role. Spinning drop experiments show that at long time scales the interface is permeable to both dissolved biopolymers and water. From droplet relaxation experiments, we could conclude that, for shorter time scales, water is the only ingredient that can diffuse through the interface. Due to this permeability, these methods cannot be used to calculate the interfacial tension accurately, without taking into account the permeability of the interface. Including the permeability, we give a full description for the relaxation time of deformed droplets. From this description, the interfacial tension and the permeability of the interface can be deduced simultaneously. We also incorporate the permeability and the bending rigidity into the description of the kinetics of phase separation. From this theoretical description, we predict four different regimes to occur in the phase-separation process depending on the size of the domains. For the scaling of the domain size with time, we find an exponent of (1)/(4) for bending- and permeability-dominated coarsening, an exponent of (1)/(3) for bending-dominated coarsening, an exponent of (1)/(2) for interfacial tension- and permeability-dominated coarsening, and an exponent of 1 for interfacial tension-dominated coarsening. The crossover between the different regimes depends on two different critical radii, R(c), equal to (2k/gamma)(1/2) and R(lambda), equal to etalambda(eff). Taking values for the interfacial properties, we find these critical radii to be larger than a micrometer, indicating that both bending rigidity and permeability are of importance during phase separation.

We discuss the coarsening of domains in bicontinuous structure of aqueous polymer mixtures, driven by hydrodynamic flow. Taking into account the bending energy as a contribution to the interfacial energy, we derive a general expression for the coarsening rate in these mixtures. Examining the limiting behavior of small and large length scales, we find two regimes. For small length scales, the size of the domains (¿) scales with time (t) as ¿ t1/3, while at large length scales, the domain size scales with time as ¿ t. The crossover between the two regimes occurs at a particular length scale, the critical radius Rc, which is dependent on the bending rigidity k, and the interfacial tension of a flat interface ¿0 (Rc = ). In the case of aqueous biopolymer mixtures, we predict this particular length scale to be in the micron range. This new general expression for the coarsening of domains in aqueous polymer mixtures can explain experimental results [Lorén et al. Macromolecules 2001, 34, 8117], which show the two regimes of coarsening with a crossover at 4 µm.