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The surface properties of aqueous dispersions of worm-like fibril aggregates of bovine serum albumin (BSA) differ from those of the adsorption layers of the native protein. The dispersions of BSA fibrils are characterized by slower changes of the surface tension and dynamic surface elasticity and also have different steady-state values of the surface properties. The fourfold compression of the adsorption layer of BSA fibrils leads to noticeably higher surface pressures than those of a compressed layer of the native protein, indicating the formation of a more rigid layer structure in the former case. The spreading of BSA fibrils onto a liquid surface from a concentrated dispersion reduces the effect of surface-active admixtures on the layer properties. The dependencies of the dynamic surface elasticity on surface pressure almost coincide for the spread layers of fibrils and the native protein in the range of low surface pressures, but only the spreading of the native protein can lead to surface pressures higher than 4 mN/m. This distinction is presumably caused by the formation of stable clusters of BSA fibrils at the interface and their slow propagation along the liquid surface.