Probing the Binding of Scutellarin to Human Serum Albumin by Circular Dichroism, Fluorescence Spectroscopy, FTIR, and Molecular Modeling Method
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- 作者：Jianniao Tian ; Jiaqin Liu ; Wenying He ; Zhide Hu ; Xiaojun Yao ; and Xingguo Chen
- 刊名：Biomacromolecules
- 出版年：2004
- 出版时间：September 2004
- 年：2004
- 卷：5
- 期：5
- 页码：1956 - 1961
- 全文大小：267K
- 年卷期：v.5,no.5(September 2004)
- ISSN：1526-4602
文摘
The binding of scutellarin with human serum albumin (HSA) was investigated at four temperatures, 296,303, 310, and 318 K, by fluorescence, circular dichroism (CD), Fourier transform infrared spectroscopy(FT-IR), and molecular modeling study at pH 7.40. The binding parameters were determined by Scatchard'sprocedure, which are approximately consistent with the results of Stern-Volmer equation. The thermodynamicparameters were calculated according to the dependence of enthalpy change on the temperature as follows:
H
is a small negative value (-8.55 kJ/mol), whereas S is a positive value (65.15 J/mol K). Quenchingof the fluorescence HSA in the presence of scutellarin was observed. Data obtained by fluorescencespectroscopy and CD experiment, FT-IR experiment, and molecular modeling method suggested thatscutellarin can strongly bind to the HSA and the primary binding site of scutellarin is located in site I ofHSA. It is considered that scutellarin binds to site I (subdomain II) mainly by a hydrophobic interaction andthere are hydrogen bond interactions between the scutellarin and the residues Arg222 and Arg257.
H is a small negative value (-8.55 kJ/mol), whereas S is a positive value (65.15 J/mol K). Quenchingof the fluorescence HSA in the presence of scutellarin was observed. Data obtained by fluorescencespectroscopy and CD experiment, FT-IR experiment, and molecular modeling method suggested thatscutellarin can strongly bind to the HSA and the primary binding site of scutellarin is located in site I ofHSA. It is considered that scutellarin binds to site I (subdomain II) mainly by a hydrophobic interaction andthere are hydrogen bond interactions between the scutellarin and the residues Arg222 and Arg257.