title: [Study on the interaction of luteolin with human serum albumin by fluorescence quenching method].
abstract: 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.
authors: College of Science, Agricultural University of Hebei, Baoding 071001, China.
authors: Zhi-Heng
authors: ZH
authors: Zhang
authors: Cai-Rui
authors: CR
authors: Li
authors: Jing-Jun
authors: JJ
authors: Ma
authors: Qiu-Hua
authors: QH
authors: Wu
authors: Chuni
authors: C
authors: Wang
authors: Qian
authors: Q
authors: Wu
authors: Zhi
authors: Z
authors: Wang
mesh_terms: 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
chemical_list: D012709:Serum Albumin; D047311:Luteolin