Fluorometric investigation on the interaction of oleanolic acid with bovine serum albumin

✍ Scribed by Zhengjun Cheng; Yuntao Zhang

• Publisher: Elsevier Science
• Year: 2008
• Tongue: English
• Weight: 565 KB
• Volume: 879
• Category: Article
• ISSN: 0022-2860
• DOI: 10.1016/j.molstruc.2007.08.020

✦ Synopsis

The interactions between oleanolic acid and bovine serum albumin (BSA) have been studied by fluorescence, circular dichroism (CD), UV-vis absorption and Fourier transform infrared spectroscopy (FTIR) under physiological conditions. Spectroscopic analysis of the emission quenching at different temperatures has revealed that the quenching mechanism of bovine serum albumin by oleanolic acid is static quenching mechanism. The binding sites number n and binding constants K are obtained at various temperatures. The distance r between oleanolic acid and the protein is evaluated according to the theory of Forster energy transfer. The results by FTIR, CD and UV-vis absorption spectra experiment indicate that the secondary structures of protein have been perturbed in the presence of oleanolic acid. The thermodynamic parameters DH 0 , DG 0 , and DS 0 are calculated according to van't Hoff equation, which indicates that the hydrogen bonds and van der-waals are the intermolecular forces stabilizing the complex. Molecular modeling studies the interaction BSA with oleanolic acid.