W/o microemulsions attract attention due to wide applications in food processing, cosmetics, drug delivery, enzymatic catalysis, organic and bio-organic reactions, etc. Knowledge of the location and state of water molecules and their diffusion in microemulsions is essential for establishing the mechanisms of extraction and solubilization, and modeling structure and phase behavior of microemulsions.In this work, we study the diffusion of water in water/n-decane microemulsions that contain nonionic surfactants Span 80 and Tween 80. We combine PGSTE NMR measurements with FT-IR spectroscopy and MD simulations for microemulsions of varying content of water, total surfactant, and Span 80 to Tween 80 ratio. Experimental NMR-data on the diffusion coefficient are reported for the temperature interval 298 – 318 K. FT-IR studies of the extent of hydrogen bonding of water and MD simulations have been performed for 298 K. We find two distinct populations of aggregates: small reverse micelles, consisting predominantly of Span80, and much larger aggregates containing considerable amounts of Tween 80. The number of water molecules in the small reverse micelles and their size remain constant with increasing water content. The size and mobility of the large aggregates depend substantially on the content of water and Tween 80. Large hydrophilic parts of Tween 80 molecules bind substantial amounts of water, massively engaged in hydrogen bonds inside the aggregate’s cores. Accumulation of water leads to swelling of these microemulsion droplets and to an increase in their size. Water pools start to appear in the droplets at ca. 8 wt.% H2O.

The dynamic properties of spread and adsorbed layers of amyloid-like silk fibroin fibrils (ALF) differ significantly from the properties of native protein layers (RSF). In the former case, the dynamic dilational surface elasticity and the steady-state adsorbed amount are considerably lower than in the latter case. This high dynamic elasticity of RSF layers is close to that of the layers of solid nanoparticles and is provided by the spontaneous formation of various interconnected supramolecular structures at the interface. The ALF produced at elevated temperatures is also intertwined at the interface but does not form a continuous network. In this case, the layer properties are close to those of the layers of amyloid fibrils of globular proteins. If the ALF dispersion is purified from admixtures of unreacted protein molecules, the dynamic surface elasticity reaches about 140 mN/m, similar to the results for dispersions of amyloid fibrils of globular proteins. The admixtures of unreacted protein molecules of high surface activity significantly influence the dynamic surface properties participating in the self-assembly, thereby leading to a slight increase in the surface elasticity. At the same time, the ALF acts as an effective inhibitor of the formation of supramolecular structures in the surface layer for mixed systems. Under the influence of amyloid fibrils, neither the impurities nor the addition of native RSF lead to mechanical surface properties close to those of native fibroin systems.