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Spectroscopic Studies on the Interaction of Asiatic Acid with Bovine Serum Albumin
Author(s) -
Yao Di,
Ni Shouhai,
Wen Maogui,
Bian Hedong,
Yu Qing,
Liang Hong,
Chen Zhenfeng
Publication year - 2011
Publication title -
chinese journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 41
eISSN - 1614-7065
pISSN - 1001-604X
DOI - 10.1002/cjoc.201190121
Subject(s) - chemistry , bovine serum albumin , enthalpy , circular dichroism , fluorescence , quenching (fluorescence) , raman spectroscopy , fluorescence spectroscopy , spectroscopy , infrared spectroscopy , fourier transform infrared spectroscopy , analytical chemistry (journal) , hydrophobic effect , crystallography , chromatography , organic chemistry , physics , quantum mechanics , optics
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 (Δ H 0 ) and entropy change (Δ S 0 ) for the reaction were evaluated to be −12.55 kJ·mol −1 and 67.08 kJ·mol −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.