Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10801109 | Biochimica et Biophysica Acta (BBA) - General Subjects | 2005 | 7 Pages |
Abstract
The interaction between Jatrorrhizine with human serum albumin (HSA) were studied by fluorescence quenching technique, circular dichroism (CD) spectroscopy, and Fourier transform infrared (FT-IR) spectroscopy. Fluorescence data revealed the presence of a single class of binding site on HSA and its binding constants (K) are 7.278Ã104, 6.526Ã104, and 5.965Ã104 L·molâ1 at 296, 303, and 310 K, respectively. The CD spectra and FT-IR spectra have proved that the protein secondary structure changed in the presence of Jatrorrhizine in aqueous solution. The effect of common ions on the binding constants was also investigated. In addition, the thermodynamic functions standard enthalpy (ÎH0) and standard entropy (ÎS0) for the reaction were calculated to be â10.891 kJ·molâ1 and 56.267 J·molâ1 Kâ1, according to the van't Hoff equation. These data indicated that hydrophobic and electrostatic interactions played a major role in the binding of Jatrorrhizine to HSA. Furthermore, the displacement experiments indicated that Jatrorrhizine could bind to the site I of HSA, which was also in agreement with the result of the molecular modeling study.
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Authors
Ying Li, Wenying He, Jiaqin Liu, Fenling Sheng, Zhide Hu, Xingguo Chen,