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Interaction of aloe-emodin with human serum albumin

Author:
JinFeng Du   Ying Li   Qi Zhang   XiaoJun Yao  


Journal:
Chinese Science Bulletin


Issue Date:
2007


Abstract(summary):

The presence of several high affinity binding sites on human serum albumin (HSA) makes it a possible target for many drugs. This study is designed to examine the effect of aloe-emodin on HSA by fluorescence, CD spectroscopy and molecular modeling. The results of fluorescence measurements suggested that the hydrophobic interaction was the predominant intermolecular force stabilizing the AE-HSA complex, which was in good agreement with the result of molecular modeling study. And the enthalpy change Delta H-0 and the entropy change Delta S-0 were calculated to be -7.041 KJ.mol(-1) and 76.619 J.mol(-1).K-1 according to the Van't Hoff equation. The alterations of protein secondary structure in the presence of AE in aqueous solution were quantitatively calculated from CD spectra, and the content of a-helices obviously increased.


Page:
200-204


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