Interaction mechanism of pelargonidin against tyrosinase by multi-spectroscopy and molecular docking

J Mol Recognit. 2022 Jun;35(6):e2955. doi: 10.1002/jmr.2955. Epub 2022 Mar 16.

Abstract

The interaction mechanism of pelargonidin (PG) with tyrosinase was investigated by multi-spectroscopy and molecular docking. As a result, PG had strong inhibitory activity on tyrosinase with the IC50 value of 41.94 × 10-6 mol·L-1 . The inhibition type of PG against tyrosinase was determined as a mixed-mode. Meanwhile, the fluorescence of tyrosinase was quenched statically by PG, and accompanied by non-radiative energy transfer. The three-dimensional (3-D) fluorescence, ultraviolet-visible spectroscopy (UV-Vis) and circular dichroism spectroscopies (CD) indicated that PG decreased the hydrophobicity of the micro-environment around tryptophan (Trp) and tyrosine (Tyr), which resulted in the conformational change of tyrosinase. In addition, fluorescence and molecular docking analysis indicated that PG bound to tyrosinase via hydrogen bonds (H-bonds) and van der Waals force (vdW force). We herein recommended that PG might be a potential candidate drug for the treatment of melanin-related diseases.

Keywords: Pelargonidin; interaction; molecular docking; multi-spectroscopy; tyrosinase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anthocyanins
  • Binding Sites
  • Circular Dichroism
  • Molecular Docking Simulation
  • Monophenol Monooxygenase* / chemistry
  • Monophenol Monooxygenase* / metabolism
  • Spectrometry, Fluorescence / methods
  • Spectrum Analysis
  • Thermodynamics

Substances

  • Anthocyanins
  • pelargonidin
  • Monophenol Monooxygenase