Issue 35, 2020, Issue in Progress

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 antiparallel β-sheet were increased. Moreover, all these experimental results were verified and reasonably explained by molecular docking results. We also investigated the enzyme activity of trypsin and the antioxidant activity of AE. The results showed that both the enzyme activity of trypsin and the antioxidant activity of AE were decreased after interaction between AE and trypsin. The findings outlined in this study should elucidate the molecular mechanisms of interaction between AE and trypsin and contribute to making full use of AE in the food industry.

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

Article information

Article type
Paper
Submitted
24 Mar 2020
Accepted
13 May 2020
First published
02 Jun 2020
This article is Open Access
Creative Commons BY license

RSC Adv., 2020,10, 20862-20871

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

G. Ren, H. Sun, G. Li, J. Fan, L. Du and G. Cui, RSC Adv., 2020, 10, 20862 DOI: 10.1039/D0RA02712J

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

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