Interaction of aloe-emodin with human serum albumin

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 fluo-rescence, CD spectroscopy and molecular modeling. The results of fluorescence measurements sug-gested 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 ΔH0 and the entropy change ΔS0 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 α-helices obviously increased.

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 △H^0 and the entropy change △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 o-helices obviously increased.