[Fluorescence spectroscopic study on the monoammonium glycyrrhizinate-bovine serum albumin supramolecular system].
The fluorescence quenching mechanism of bovine serum albumin (BSA) by monoammoniumglycyrrhizinate (MAG) has been studied. It is proved that static quenching exists in the MAG-BSA supramolecular complex. The formation constant KA and the thermodynamic functions (such as deltaG, deltaH and deltaS) for the reaction have been all obtained. According to the thermodynamic parameters, the main sort of binding force was electrostatic force. The effect of various metal ions and temperatures on the formation constant of MAG with BSA was also studied. The binding distance between MAG and BSA and the transfer efficiency have been obtained based on the mechanism of Forster energy transfer. The effect of MAG on the conformation of BSA has also been analyzed using synchronous fluorescence spectroscopy.
Yu
Yin
Y
College of Material Science and Engineering, South China University of Technology, Guangzhou 510640, China.
Zhou
Zhen-tao
ZT
D000818:Animals; D002417:Cattle; D004735:Energy Transfer; D019695:Glycyrrhizic Acid / Q000031:analogs & derivatives* / Q000737:chemistry* / Q000378:metabolism; D007700:Kinetics; D008670:Metals / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology; D011485:Protein Binding / Q000187:drug effects; D012710:Serum Albumin, Bovine / Q000737:chemistry* / Q000378:metabolism; D013050:Spectrometry, Fluorescence; D055672:Static Electricity; D013696:Temperature; D013816:Thermodynamics
D008670:Metals; D012710:Serum Albumin, Bovine; D019695:Glycyrrhizic Acid