Study of the interaction between monoammonium glycyrrhizinate and bovine serum albumin.
The interaction between monoammonium glycyrrhizinate (MAG) and bovine serum albumin (BSA) were studied by fluorescence and absorption spectroscopy. The quenching mechanism of fluorescence of bovine serum albumin by monoammonium glycyrrhizinate was discussed. The binding sites number n and apparent binding constant K were measured by fluorescence quenching method. The thermodynamic parameters DeltaH degrees , DeltaG degrees , DeltaS degrees at different temperatures were calculated. The distance r between donor (bovine serum albumin) and acceptor (monoammonium glycyrrhizinate) was obtained according to Forster theory of non-radiation energy transfer. The results of synchronous fluorescence spectra and UV-vis absorption spectra show that the conformation of bovine serum albumin has been changed.
Hu
Yan-Jun
YJ
Department of Chemistry, College of Chemistry and Molecular Sciences, Wuhan University, Wuhan 430072, PR China.
Liu
Yi
Y
Wang
Jia-Bo
JB
Xiao
Xiao-He
XH
Qu
Song-Sheng
SS
D000818:Animals; D002417:Cattle; D004347:Drug Interactions; D019695:Glycyrrhizic Acid / Q000032:analysis / Q000737:chemistry / Q000378:metabolism*; D000644:Quaternary Ammonium Compounds / Q000032:analysis / Q000737:chemistry / Q000378:metabolism*; D012710:Serum Albumin, Bovine / Q000032:analysis / Q000378:metabolism*; D013056:Spectrophotometry, Ultraviolet / Q000379:methods
D000644:Quaternary Ammonium Compounds; D012710:Serum Albumin, Bovine; D019695:Glycyrrhizic Acid