Amyloids, a well-ordered b-sheet-enriched structural network, can be broadly defined as insoluble protein aggregates that are linked to a wide variety of diseases including systemic amyloidosis and some neurodegenerative disorders. Ferulic acid (FA), a phenolic acid, abundant in antioxidant and efficientpharmaceutical has beneficial effects against several ailments. Based on this, we have investigated the protective role of FA on amyloid formation of bovine b-lactoglobulin (b-lg), a model globular protein. Using a set of in vitro biophysical methods, such as UV-Vis spectroscopy, fluorescence, circular dichroism,transmission electron microscopy, etc., our research group has concluded that FA significantly inhibits the heat-induced amyloid formation of b-lg and this inhibitory effect is dose-dependent. Exposed surface hydrophobicity of b-lg amyloid fibrils decreased significantly in the presence of FA. Docking study revealed that ionic and hydrogen bonding interactions between FA and b-lg prevented protein conformational changes leading to fibrillation. We anticipate that our finding would give an insight into the protein aggregation inhibited by the antioxidant compound, FA and pave the way for finding and developing other new small molecules (protein misfolding inhibitors) that give similar result against amyloid fibril formation and its allied neurodegenerative disorders.