Background: Ionizing radiation causes deleterious effects on living system mainly due to oxidative damages of macromolecules and protein is the major target due to its abundance. The aim of this study was to investigate the effects of ionizing radiation induced changes in the molecular properties of bovine serum albumin (BSA) its secondary and tertiary structures, degradation, cross linking and radioprotective role of ferulic acid, a natural antioxidant on these radiation induced changes. Materials and Methods: This study was carried out to investigate the gamma radiation induced oxidative, structural damage of BSA and radioprotective efficacy of ferulic acid through SDS-PAGE, DTNB assay, DNPH assay, FOX assay methods. Hydroxyl radical scavenging capacity of ferulic acid was estimated using 2-deoxy ribose assay. Further, radiation induced changes in the anisotropy and excitation state lifetimes of BSA were examined. Results: SDS –PAGE data suggested that the loss of protein was linearly dependent on the radiation dose. Gamma-irradiation of BSA caused the formation of protein carbonyls, hydroperoxides and loss of thiols. Ferulic acid protected the radiation induced loss of protein as well as reduced various oxidative damages. Ferulic acid protected the protein from radiation induced damages in a concentration dependent manner. Conclusion: The results provide insight into radiation induced molecular changes in the protein. Ferulic acid protected the BSA from oxidative modification caused by radiation suggesting that ferulic acid possesses strong antiradical properties. Ferulic acid is known to protect DNA, the prime target of radiation and further its ability to protect protein suggesting its ability to protect different biomolecules and therefore can be a good candidate for development radioprotector.