期刊
MOLECULAR NUTRITION & FOOD RESEARCH
卷 54, 期 -, 页码 S253-S260出版社
WILEY
DOI: 10.1002/mnfr.200900454
关键词
7-Hydroxyflavone; Baicalein; Chrysin; Flavone; Serum albumins
资金
- Natural Science Foundation of Shanghai [10ZR1421700]
- Shanghai Municipal Education Commission [10YZ68]
- Shanghai Education Development Foundation [09CG46]
- National Natural Science Foundation of China [20775092]
- National High Technology Research and Development (863) Program of China [2008AA10Z322]
Four flavones (flavone, 7-hydroxyflavone, chrysin, and baicalein) sharing the same B- and C-ring structure but a different numbers of hydroxyl groups on the A-ring were studied for their affinities for BSA and HSA. The hydroxylation on ring A of flavones increased the binding constants (K-a) and the number of binding sites (n) between flavones and serum albumins. The affinities of 7-hydroxyflavone for BSA and HSA were about 800 times and 40 times higher than that of flavone, respectively. It appears that the optimal number of hydroxyl groups introduced to the ring A of flavones is one. As more hydroxyl groups were introduced to positions at C-5, C-6, and/or C-7 of flavones, the affinities for serum albumins decrease. The critical energy transfer distances (R-0) between the hydroxylated flavones (1-3 OH on the ring A) and serum albumins decreased with the increasing affinities for serum albumins.
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