Abstract <p>Destabilization of protein structures that leads to subsequent self-association with the formation of amyloid fibrils underlies several neurodegenerative diseases. Many studies aim to identify effective inhibitors of this process. This work examines the inhibitory action of natural nontoxic amphiphilic compounds that form liposomes on the formation of fibrils by serum albumin. The specific dye thioflavin T was used to evaluate kinetic parameters. Changes in the protein structure during its interaction with liposomes were monitored by IR and fluorescence spectroscopy. Particle sizes present in solution were assessed by dynamic light scattering. Liposomes were found to have almost no effect on the rate of fibril formation, although they reduced the amount of fibrils by binding destabilized forms of the protein and intermediate aggregates.</p>