Interaction of bovine serum albumin with luteolin and apigenin.
- Author:
Ling-bo QU
1
;
Ling WANG
;
Ran YANG
;
Xiao-lan CHEN
;
Ping LI
Author Information
- Publication Type:Journal Article
- MeSH: Apigenin; chemistry; Energy Transfer; Luteolin; chemistry; Protein Binding; Serum Albumin, Bovine; chemistry; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Thermodynamics
- From: Acta Pharmaceutica Sinica 2006;41(4):352-357
- CountryChina
- Language:Chinese
-
Abstract:
AIMTo study the interaction mechanism of bovine serum albumin (BSA) with luteolin and apigenin.
METHODSFluorescence quenching method and non-radioactive energy transfer theory were used.
RESULTSThe 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.
CONCLUSIONThe 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.
