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Study on the mechanism of the interaction between acteoside and pepsin using spectroscopic techniques
Author(s) -
Fang Yifeng,
Xu Hong,
Shen Liangliang,
Huang Fengwen,
Yibulayin Shadaiti,
Huang Songyang,
Tian Shengli,
Hu Zhangli,
He Zhendan,
Li Fangrong,
Li Yig,
Zhou Kai
Publication year - 2015
Publication title -
luminescence
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.428
H-Index - 45
eISSN - 1522-7243
pISSN - 1522-7235
DOI - 10.1002/bio.2833
Subject(s) - chemistry , fluorescence , quenching (fluorescence) , pepsin , van der waals force , spectral line , hydrogen bond , fluorescence spectroscopy , photochemistry , absorption spectroscopy , absorption (acoustics) , analytical chemistry (journal) , chromatography , molecule , organic chemistry , enzyme , quantum mechanics , astronomy , acoustics , physics
The interaction of acteoside with pepsin has been investigated using fluorescence spectra, UV/vis absorption spectra, three‐dimensional (3D) fluorescence spectra and synchronous fluorescence spectra, along with a molecular docking method. The fluorescence experiments indicate that acteoside can quench the intrinsic fluorescence of pepsin through combined quenching at a low concentration of acteoside, and static quenching at high concentrations. Thermodynamic analysis suggests that hydrogen bonds and van der Waal's forces are the main forces between pepsin and acteoside. According to the theory of Förster's non‐radiation energy transfer, the binding distance between pepsin and acteoside was calculated to be 2.018 nm, which implies that energy transfer occurs between acteoside and pepsin. In addition, experimental results from UV/vis absorption spectra, 3D fluorescence spectra and synchronous fluorescence spectra imply that pepsin undergoes a conformation change when it interacts with acteoside. Copyright © 2015 John Wiley & Sons, Ltd.