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.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
