Investigation on the binding of aloe-emodin with tyrosinase by spectral analysis and molecular docking.

Abstract

In this paper, the inhibitory kinetics of aloe-emodin on the activity of tyrosinase and the inhibitory mechanism have been investigated by using spectroscopic and molecular docking techniques. The results showed that aloe-emodin inhibited tyrosinase activity in a competitive manner. The binding constants, number of binding sites and thermodynamic parameters obtained at different temperature suggested that aloe-emodin spontaneously binds to tyrosinase at one binding site, mainly via electrostatic forces. Analysis by UV-vis absorption (UV), circular dichroism (CD) and molecular docking indicated that aloe-emodin bound directly into the catalytic cavity and that binding of aloe-emodin to tyrosinase induced conformational changes of the enzyme and blocked the catalytic center of the enzyme preventing binding of the substrate, which caused the inhibition of the tyrosinase activity.