Authors: Jiaqin Liu Jianniao Tian Jiyou Zhang Zhide Hu Xingguo Chen
Publish Date: 2003/06/27
Volume: 376, Issue: 6, Pages: 864-867
Abstract
The interaction of magnolol with bovine serum albuminBSA was studied using fluorescence spectroscopy under physiological conditions The binding constants K and the ratio of quantum yields of protein fluorescence for complex and free protein f at 298 K 304 K and 310 K were obtained the values were 6799×105 L mol−1 5541×105 L mol−1 and 4344×105 L mol−1 and 017 030 and 034 respectively The standard enthalpy change ΔH° and the standard entropy change ΔS° were calculated to be –2853 kJ mol−1 and 1588 J mol−1 K−1 which indicated that hydrophobic forces played major role in the interaction of magnolol and BSA The binding average distance between magnolol and BSA 432 nm was obtained on the basis of the theory of Förster energy transfer
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