Formation of a Multiligand Complex of Bovine Serum Albumin with Retinol, Resveratrol, and (−)-Epigallocatechin-3-gallate for the Protection of Bioactive Components

Bovine serum albumin Gallate Serum Albumin
DOI: 10.1021/acs.jafc.7b00326 Publication Date: 2017-03-24T15:25:26Z
ABSTRACT
Clarification of the interaction mechanisms between proteins and bioactive components is important to develop effective carriers for encapsulation protection components. Bovine serum albumin (BSA), a globular protein in milk, contains multiple sites bind variety low-molecular-weight molecules, forming protein-monoligand complexes. In this study, interactions BSA with retinol, resveratrol, and/or (-)-epigallocatechin-3-gallate (EGCG) were investigated by using fluorescence, circular dichroism, molecular docking techniques. BSA-triligand complexes successfully formed when added sequence EGCG. The stability these was improved relative free ones. provided better protective effect on retinol resveratrol than did BSA-monoligand complexes, which presence EGCG played an role.
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