Spectroscopic Studies on the Interaction of Asiatic Acid with Bovine Serum Albumin |
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Authors: | Yao Di Ni Shouhai Wen Maogui Bian Hedong Yu Qing Liang Hong Chen Zhenfeng |
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Institution: | Key Laboratory for Chemistry and Molecular Engineering of Medicinal Resources (Guangxi Normal University), Ministry of Education of China, Guilin, Guangxi 541004, China |
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Abstract: | 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 (ΔH0) and entropy change (ΔS0) 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. |
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Keywords: | bovine serum albumin asiatic acid secondary structure fluorescence spectroscopy fourier transform infrared (FT‐IR) circular dichroism raman spectroscopy |
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