Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 59, Issue 19, Pages 10761-10769Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jf2027523
Keywords
binding affinity; bovine serum albumin; chemical structure; flavonoid; flavonoid-Cu2+ complex
Funding
- National Scientific Foundation of China [21005089]
- Natural Science Foundation of Hunan Province of China [10JJ4006]
- Central South University [201012200015]
- State Key Laboratory of Powder Metallurgy
- aid program for Science and Technology Innovative Research Team (Chemicals of Forestry Resources and Development of Forest Products) in Higher Educational Institutions of Hunan Province
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The effects of 1:1 flavonoid-Cu2+ complexes of four flavonoids with different C-ring substituents, quercetin (QU), luteolin (LU), taxifolin (TA), and (+)-catechin (CA), on bovine serum albumin (BSA) were investigated and compared with corresponding free flavonoids by spectroscopic analysis in an attempt to characterize the chemical association taking place. The results indicated that all of the quenching mechanisms were based on static quenching combined with nonradiative energy transfer. Cu2+ chelation changed the binding constants for BSA depending on the structures of flavonoids and the detected concentrations. The reduced hydroxyl groups, increased steric hindrance, and hydrophilicity of Cu2+ chelation may be the main reasons for the reduced binding constants, whereas the formation of stable flavonoid-Cu2+ complexes and synergistic action could increase the binding constants. The changed trends of critical energy transfer distance (R-0) for Cu2+ chelation were contrary to those of binding constants.
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