[Interaction of bovine serum albumin with luteolin and apigenin].
OBJECTIVE
To study the interaction mechanism of bovine serum albumin (BSA) with luteolin and apigenin.


METHODS
Fluorescence quenching method and non-radioactive energy transfer theory were used.


RESULTS
The binding constants at different temperature were determined and the quenching mechanism of them were suggested as static quenching. The transfer efficiency of energy and distance between BSA and luteolin or apigenin were investigated according to the mechanism of the Förster energy transference.


CONCLUSIONS
The interaction between them seems to be strong and the binding force were mainly hydrophobic force. B(3')-OH,B(4')-OH strengthened the interaction of flavonoids and BSA.
Qu
Ling-bo
LB
Department of Chemistry, Zhengzhou University, China. qulingbo@zzu.edu.cn
Wang
Ling
L
Yang
Ran
R
Chen
Xiao-lan
XL
Li
Ping
P
D047310:Apigenin / Q000737:chemistry*; D004735:Energy Transfer; D047311:Luteolin / Q000737:chemistry*; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D013816:Thermodynamics
D012710:Serum Albumin, Bovine; D047310:Apigenin; D047311:Luteolin