期刊
FOOD CHEMISTRY
卷 301, 期 -, 页码 -出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2019.125294
关键词
(-)-Epigallocatechin-3-gallate; Bovine serum albumin; Fluorescence; HPLC; Docking studies
资金
- National Key Research and Development Plan [2018YFD0600404]
- Program of Innovative Research Team in Institute of Chemical Industry of Forest Products, CAF [LHSXKQ4]
The interaction of copper complexed with (-)-epigallocatechin-3-gallate (EGCG) and bovine serum albumin (BSA) was investigated using fluorescence, circular dichroism (CD) spectroscopy, HPLC and protein-ligand docking. The fluorescence quenching efficiency of BSA by EGCG was enhanced after EGCG was complexed with copper, and the EGCG-Cu complex exhibited a higher apparent binding affinity (8.88 x 10(5) M-1) to BSA compared with EGCG alone (5.17 x 10(5) M-1). The CD experiment showed that both the EGCG-BSA and [EGCGCu]-BSA interactions resulted in the unfolding of the secondary structure of the protein. Results of competitive binding experiments confirmed that the location of EGCG and EGCG-Cu complex binding in BSA was site I. Furthermore, molecular modeling was used to identify the amino acid residue in site I and site II that play key roles in this binding interaction. The data suggest that most of the residues involved in the [EGCG-Cu]-BSA reaction belong to the subdomains Ha (site I) of BSA.
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