Abstract
Punicalagin has been attracted much attention owing to its biological activity of regulating blood glucose and potential as a health benefits. Herein, the binding behavior of punicalagin with pepsin were investigated by spectrofluorometric, UV–Vis spectrophotometric, synchronous fluorescence, three-dimensional (3-D) fluorescence, circular dichroism (CD), UV–Vis, Fourier transform infrared (FT-IR), docking examinations and molecular dynamics simulation. Fluorescence spectroscopy reveals that punicalagin spontaneously binds to pepsin and quenches the intrinsic fluorescence of pepsin. According to the results of steady-state fluorescence and fluorescence lifetime, the quenching mechanism of punicalagin and pepsin was static quenching. Synchronous fluorescence spectroscopy, 3-D fluorescence, CD, UV–Vis and FT-IR demonstrated that it induced conformational alterations of pepsin in the presence of punicalagin. Complementary molecular docking and dynamics simulations elucidated that the binding of pepsin and punicalagin occurred via establishment of hydrogen-bonding and Van der Waals interactions. This work provided some important information for further research on punicalagin-proteases interactions, which contributed to the activity and binding mechanism of punicalagin and pepsin in future.
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