Spectroscopic Studies on the Interaction of Asiatic Acid with Bovine Serum Albumin  

作　　者：Yao, Di Ni, Shouhai Wen, Maogui Bian, Hedong Yu, Qing Liang, Hong Chen, Zhenfeng 

机构地区：[1]Key Laboratory for Chemistry and Molecular Engineering of Medicinal Resources (Guangxi Normal University), Ministry of Education of China, Guilin, Guangxi 541004, China

出　　处：《Chinese Journal of Chemistry》2011年第3期549-554,共6页中国化学（英文版）

基　　金：Project supported by the National Natural Science Foundation of China （Nos. 20671023, 30460153, 21061002）, the Key Project of Chinese Ministry of Education （Nos. 03101, 204111）, Guangxi Natural Science Foundation of China （No. 2010GXNSFF013001）, and the Innovation Project of Guangxi Graduate Education （No. 2009106020703M42）.

摘　　要：Fluorescence spectroscopy, Fourier transform infrared （FT-IR） spectroscopy, circular dichroism （CD） and FT-Raman spectroscopy were employed to analyze the binding of the asiatic acid （AA） to bovine serum albumin （BSA） under simulative physiological conditions. Fluorescence data revealed that the fluorescence quenching of BSA by AA was the result of the formation of BSA-AA complex. The fluorescence quenching mechanism of BSA by AA was a static quenching procedure. According to the Van＇t Hoff equation, the thermodynamic parameters enthalpy change （△H0） and entropy change （△S0） for the reaction were evaluated to be --12.55 kJ·mol^-1 and 67.08 kJomol 1, respectively, indicating that hydrophobic and electrostatic interactions played a major role in stabilizing the complex. The influence of AA on the conformation of BSA has also been analyzed on the basis of FT-IR, CD and FT-Raman spectra.Fluorescence spectroscopy, Fourier transform infrared （FT-IR） spectroscopy, circular dichroism （CD） and FT-Raman spectroscopy were employed to analyze the binding of the asiatic acid （AA） to bovine serum albumin （BSA） under simulative physiological conditions. Fluorescence data revealed that the fluorescence quenching of BSA by AA was the result of the formation of BSA-AA complex. The fluorescence quenching mechanism of BSA by AA was a static quenching procedure. According to the Van＇t Hoff equation, the thermodynamic parameters enthalpy change （△H0） and entropy change （△S0） for the reaction were evaluated to be --12.55 kJ·mol^-1 and 67.08 kJomol 1, respectively, indicating that hydrophobic and electrostatic interactions played a major role in stabilizing the complex. The influence of AA on the conformation of BSA has also been analyzed on the basis of FT-IR, CD and FT-Raman spectra.

关 键 词：bovine serum albumin asiatic acid secondary structure fluorescence spectroscopy fourier transforminfrared （FT-IR） circular dichroism raman spectroscopy 

分 类 号：O647.2[理学—物理化学] Q512.1[理学—化学]