LAUSR

Clarification of the interaction mechanisms between proteins and bioactive components is important to develop effective carriers for encapsulation and protection of bioactive components. Bovine serum albumin (BSA), a globular protein in serum and milk, contains multiple sites to bind a variety of low-molecular-weight molecules, forming protein-monoligand complexes. In this study, the interactions of BSA with retinol, resveratrol, and/or (-)-epigallocatechin-3-gallate (EGCG) were investigated by using fluorescence, circular dichroism, and molecular docking techniques. BSA-triligand complexes were successfully formed when added in the sequence of retinol, resveratrol, and EGCG. The stability of these bioactive components was improved in the complexes relative to free ones. The complexes provided a better protective effect on retinol and resveratrol than did BSA-monoligand complexes, in which the presence of EGCG played an important role.