1. Investigation on interaction between Ligupurpuroside A and pepsin by spectroscopic and docking methods.
- Author
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Shen, Liangliang, Xu, Hong, Huang, Fengwen, Li, Yi, Xiao, Huafeng, Yang, Zhen, Hu, Zhangli, He, Zhendan, Zeng, Zheling, and Li, Yinong
- Subjects
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PEPSIN , *MOLECULAR docking , *GLYCOSIDES , *FLUORESCENCE spectroscopy , *ENERGY transfer , *HYDROGEN bonding , *PROTEIN-ligand interactions - Abstract
Ligupurpuroside A is one of the major glycoside in Ku-Din-Cha, a type of Chinese functional tea. In order to better understand its digestion and metabolism in humans, the interaction between Ligupurpuroside A and pepsin has been investigated by fluorescence spectra, UV–vis absorption spectra and synchronous fluorescence spectra along with molecular docking method. The fluorescence experiments indicate that Ligupurpuroside A can effectively quench the intrinsic fluorescence of pepsin through a combined quenching way at the low concentration of Ligupurpuroside A, and a static quenching procedure at the high concentration. The binding constant, binding sites of Ligupurpuroside A with pepsin have been calculated. The thermodynamic analysis suggests that non-covalent reactions, including electrostatic force, hydrophobic interaction and hydrogen bond are the main forces stabilizing the complex. According to the Förster’s non-radiation energy transfer theory, the binding distance between pepsin and Ligupurpuroside A was calculated to be 3.15 nm, which implies that energy transfer occurs between pepsin and Ligupurpuroside A. Conformation change of pepsin was observed from UV–vis absorption spectra and synchronous fluorescence spectra under experimental conditions. In addition, all these experimental results have been validated by the protein-ligand docking studies which show that Ligupurpuroside A is located in the cleft between the domains of pepsin. [ABSTRACT FROM AUTHOR]
- Published
- 2015
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