sina khodarahmi

Curcumin is a natural polyphenolic compound with anti-cancer, anti-inflammatory, and anti-oxidation properties. Low water solubility and rapid hydrolytic degradation are two challenges limiting use of curcumin as therapeutic agent. In the current study, the role of the native/modified forms of bovine serum albumin (BSA) and casein, as food-grade biopolymers and safe drug delivery systems, on the physical and biological activity of curcumin were surveyed. Analyses of quenching of proteins fluorescence by curcumin indicated that chemical modification decreased binding affinity of curcumin toward albumin whereas it significantly increased for casein and average number of binding sites also doubled in modified casein. Measurement of cell viability using LDH assay showed that cytotoxicity of protein-bound curcumin is higher than free curcumin. Moreover, in the presence of native proteins, curcumin revealed elevated in vitro anti-cancer activity (against MCF7 and SKNMC) compared to modified forms. It appears that BSA and casein as protein vehicles are useful tools to increase both food quality and the bioavailability of curcumin as health promoting agent. However, results imply that the chemical modification of proteins cannot improve the anti-cancer activity of curcumin despite increasing of their binding affinity.