[Study on the interaction of luteolin with human serum albumin by fluorescence quenching method].
The interaction between luteolin and human serum albumin (HSA) was studied by using fluorescence quenching spectra, synchronous fluorescence spectra and ultra-violet spectra. The results showed that luteolin had a strong ability to quench the fluorescence of HAS The Stern-Volmer curve of the fluorescence quenching of HSA by luteolin indicated that the mechanism behind the quenching between luteolin and HSA was a static quenching. According to the Forster theory of non-radiation energy transfer, the binding distances (r) and the binding constants (KA) were calculated. The thermodynamic parameters showed that the interaction between luteolin and HSA was driven mainly by hydrophobic force. Synchronous spectra were used to investigate the conformational changes of HSA.
Zhang
Zhi-Heng
ZH
College of Science, Agricultural University of Hebei, Baoding 071001, China.
Li
Cai-Rui
CR
Ma
Jing-Jun
JJ
Wu
Qiu-Hua
QH
Wang
Chuni
C
Wu
Qian
Q
Wang
Zhi
Z
D006801:Humans; D047311:Luteolin / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D012709:Serum Albumin / Q000737:chemistry*; D013050:Spectrometry, Fluorescence / Q000379:methods*; D013056:Spectrophotometry, Ultraviolet; D013816:Thermodynamics
D012709:Serum Albumin; D047311:Luteolin