Interaction mechanism of aloe-emodin with trypsin: molecular structure-affinity relationship and effect on biological activities.

ABSTRACT: The molecular mechanism of interaction between aloe-emodin (AE) and trypsin was investigated, exhibiting remarkable outcomes. To detect the interaction mechanism, the binding of AE with trypsin was examined by a multi-spectroscopy and molecular docking method. Results showed that the binding of AE and trypsin would lead to static quenching and their binding forces were van der Waals forces and hydrogen bonding. The results of simultaneous and three-dimensional fluorescence spectroscopy showed that the combination of AE and trypsin caused changes in the microenvironment around the trypsin fluorophore, which might change the spatial structure of trypsin. FT-IR spectroscopy showed that the contents of α-helix and β-turn in trypsin were decreased and the contents of β-sheet, random coil and an

SUBMITTER: Ren G 

PROVIDER: S-EPMC9054315 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature