The binding of （-）-epigallocatechin-3-O-gallate （EGCG） to bovine serum albumin （BSA） were investigated for the first time with spectral methods, including fluorescence and absorption spectrometry under simulativ...The binding of （-）-epigallocatechin-3-O-gallate （EGCG） to bovine serum albumin （BSA） were investigated for the first time with spectral methods, including fluorescence and absorption spectrometry under simulative physiological conditions. A strong fluorescence quenching reaction of EGCG to BSA was observed. It was proved that the fluorescence quenching of BSA by addition of EGCG was a result of the formation of EGCG-BSA complex. The binding constant K and the number of binding sites n were determined at physiological conditions and three different temperatures with fluorescence quenching method. The binding distance R and transfer efficiency E between BSA and EGCG were also obtained according to Forster theory of non-radiation energy transfer. The effects of Al^3＋, Cu^2＋, Mg^2＋ and Fe^2＋ on the binding constant between EGCG and BSA were studied at 298 K. The effect of EGCG on the conformation of BSA was also analyzed by synchronous fluorescence spectroscopy. PACS. 21. 10. Dr; 32. 50. ＋d; 32. 30. Jc; 82.80. Dx展开更多
文摘The binding of （-）-epigallocatechin-3-O-gallate （EGCG） to bovine serum albumin （BSA） were investigated for the first time with spectral methods, including fluorescence and absorption spectrometry under simulative physiological conditions. A strong fluorescence quenching reaction of EGCG to BSA was observed. It was proved that the fluorescence quenching of BSA by addition of EGCG was a result of the formation of EGCG-BSA complex. The binding constant K and the number of binding sites n were determined at physiological conditions and three different temperatures with fluorescence quenching method. The binding distance R and transfer efficiency E between BSA and EGCG were also obtained according to Forster theory of non-radiation energy transfer. The effects of Al^3＋, Cu^2＋, Mg^2＋ and Fe^2＋ on the binding constant between EGCG and BSA were studied at 298 K. The effect of EGCG on the conformation of BSA was also analyzed by synchronous fluorescence spectroscopy. PACS. 21. 10. Dr; 32. 50. ＋d; 32. 30. Jc; 82.80. Dx
