| Author |
Fang, Yifeng Xu, Hong Shen, Liangliang Huang, Fengwen Yibulayin, Shadaiti Huang, Songyang Tian, Shengli Hu, Zhangli He, Zhendan Li, Fangrong Li, Yinong Zhou, Kai |
| Description |
Country affiliation: China Author Affiliation: Fang Y ( College of Life Sciences, Shenzhen Key Laboratory of Marine Bioresources and Ecology/Shenzhen Key Laboratory of Microbial Genetic Engineering, Shenzhen University, Shenzhen, 518060, China.); Xu H ( College of Life Sciences, Shenzhen Key Laboratory of Marine Bioresources and Ecology/Shenzhen Key Laboratory of Microbial Genetic Engineering, Shenzhen University, Shenzhen, 518060, China.); Shen L ( College of Life Sciences, Shenzhen Key Laboratory of Marine Bioresources and Ecology/Shenzhen Key Laboratory of Microbial Genetic Engineering, Shenzhen University, Shenzhen, 518060, China.); Huang F ( College of Life Sciences, Shenzhen Key Laboratory of Marine Bioresources and Ecology/Shenzhen Key Laboratory of Microbial Genetic Engineering, Shenzhen University, Shenzhen, 518060, China.); Yibulayin S ( College of Life Sciences, Shenzhen Key Laboratory of Marine Bioresources and Ecology/Shenzhen Key Laboratory of Microbial Genetic Engineering, Shenzhen University, Shenzhen, 518060, China.); Huang S ( College of Life Sciences, Shenzhen Key Laboratory of Marine Bioresources and Ecology/Shenzhen Key Laboratory of Microbial Genetic Engineering, Shenzhen University, Shenzhen, 518060, China.); Tian S ( College of Life Sciences, Shenzhen Key Laboratory of Marine Bioresources and Ecology/Shenzhen Key Laboratory of Microbial Genetic Engineering, Shenzhen University, Shenzhen, 518060, China.); Hu Z ( College of Life Sciences, Shenzhen Key Laboratory of Marine Bioresources and Ecology/Shenzhen Key Laboratory of Microbial Genetic Engineering, Shenzhen University, Shenzhen, 518060, China.); He Z ( School of Medicine, Shenzhen University, Shenzhen, 518060, China.); Li F ( Shenzhen Entry-Exit inspection and Quarantine Bureau, Shenzhen, 518001, China.); Li Y ( Shenzhen Entry-Exit inspection and Quarantine Bureau, Shenzhen, 518001, China.); Zhou K ( Shenzhen Marine Environment and Resource Monitoring Center, Shenzhen, 518060, China.) |
| Abstract |
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. |
