Effects of zinc binding on the binding of epigallocatechin gallate (green tea) to bovine serum albumin and myoglobin.

Abstract Serum albumin as a zinc carrier binds 80% plasma zinc to facilitate zinc absorption. Epigallocatechin gallate (EGCG, green tea) is reported to bind to serum albumin to perform its biological functions in vivo. However, the available information on how zinc binding affects the binding of EGCG to proteins or how EGCG binding affects the binding of zinc to proteins are very limited. In the present study, the effects of zinc binding on the binding of EGCG to bovine serum albumin and myoglobin were investigated using isothermal titration calorimetry, fluorescence quenching and molecular docking. The obtained results suggested that binding of zinc to bovine serum albumin and myoglobin could increase the EGCG binding affinity of proteins as indicated by the thermodynamic parameters. In addition, the formation of protein/zinc complex shifted the EGCG binding site of proteins. For myoglobin, the electron transfer from EGCG to myoglobin was facilitated by zinc binding induced stronger EGCG binding to myoglobin. Such study provides very fundamental and useful knowledge for zinc and EGCG nutrition.