The dynamic surface properties of α-lactalbumin (ALA) aqueous dispersions differ noticeably from the properties of fibril dispersions of other globular proteins. Unlike the fibrils of β-lactoglobulin and lysozyme, ALA fibrils can be easily purified from hydrolyzed peptides and native protein molecules. The dynamic surface elasticity of ALA fibril dispersions exceeds the surface elasticity of native protein solutions at pH 2. ALA fibrils proved to be stable at this pH but the stability breaks at higher pH when the fibrils start to release small peptides of high sur-face activity. As a result the dynamic surface properties of ALA coincide with those of native protein solutions. The ionic strength influences strongly the adsorption kinetics of both fibril dispersions and native protein solutions but have almost no impact on the structure of the ad-sorption layers.