Protein molecule stratification inside a single curved film: Evidence from X-ray scattering

Abstract

We have studied single curved films stabilized by globular proteins, using small angle scattering. By combining both the use of in-house X-ray and synchrotron radiation, we have measured the structural properties of films (thickness, electronic density) by controlling the physicochemical properties of protein (ovalbumin, pH 7, bulk concentration 10 g L⁻¹). For each experiment, solutions of highly purified protein were freshly prepared to eliminate any problem of aging. The observation of Kiessig fringes shows that the films are thin with an average thickness of 60 nm. Benefiting from the fine angular resolution and the short acquisition time of a synchrotron source, we have highlighted a stratification formation inside the films. This phenomenon suggests protein structural reorganization under confinement, possibly driven by high osmotic pressure.