title: [Interaction of bovine serum albumin with luteolin and apigenin].
abstract: 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.
authors.affiliation: Department of Chemistry, Zhengzhou University, China. qulingbo@zzu.edu.cn
authors.forename: Ling-bo
authors.initials: LB
authors.lastname: Qu
authors.forename: Ling
authors.initials: L
authors.lastname: Wang
authors.forename: Ran
authors.initials: R
authors.lastname: Yang
authors.forename: Xiao-lan
authors.initials: XL
authors.lastname: Chen
authors.forename: Ping
authors.initials: P
authors.lastname: Li
mesh_terms: 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
chemical_list: D012710:Serum Albumin, Bovine; D047310:Apigenin; D047311:Luteolin