Spectroscopic characterization of effective components anthraquinones in Chinese medicinal herbs binding with serum albumins.
The interactions of serum albumins such as human serum albumin (HSA) and bovine serum albumin (BSA) with emodin, rhein, aloe-emodin and aloin were assessed employing fluorescence quenching and absorption spectroscopic techniques. The results obtained revealed that there are relatively strong binding affinity for the four anthraquinones with HSA and BSA and the binding constants for the interactions of anthraquinones with HSA or BSA at 20 degrees C were obtained. Anthraquinone-albumin interactions were studied at different temperatures and in the presence of some metal ions. And the competition binding of anthraquinones with serum albumins was also discussed. The Stern-Volmer curves suggested that the quenching occurring in the reactions was the static quenching process. The binding distances and transfer efficiencies for each binding reactions were calculated according to the Föster theory of non-radiation energy transfer. Using thermodynamic equations, the main action forces of these reactions were also obtained. The reasons of the different binding affinities for different anthraquinone-albumin reactions were probed from the point of view of molecular structures.
Bi
Shuyun
S
College of Chemistry, Jilin University, Linyuan Road 1788, Changchun 130023, PR China.
Song
Daqian
D
Kan
Yuhe
Y
Xu
Dong
D
Tian
Yuan
Y
Zhou
Xin
X
Zhang
Hanqi
H
D000880:Anthraquinones / Q000032:analysis* / Q000097:blood* / Q000737:chemistry; D001665:Binding Sites; D004365:Drugs, Chinese Herbal / Q000737:chemistry*; D004642:Emodin / Q000031:analogs & derivatives / Q000737:chemistry; D006801:Humans; D008958:Models, Molecular; D015394:Molecular Structure; D012709:Serum Albumin / Q000378:metabolism*; D012710:Serum Albumin, Bovine / Q000378:metabolism
D000880:Anthraquinones; D004365:Drugs, Chinese Herbal; D012709:Serum Albumin; D012710:Serum Albumin, Bovine; C518327:aloe emodin; D004642:Emodin; C006457:alloin; C020491:rhein