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.
Milyaeva et al. (Thu,) studied this question.