In silico and in vitro Antityrosinase Activity of the Non-Protein Fraction from the Sericin Extract of Antheraea proylei J.

Background

Tyrosinase is an enzyme involved in the production of L-DOPA. To look for novel tyrosinase inhibitors, we investigated the non-protein fraction from the sericin extract of the silk cocoon shell of Antheraea proylei J. for its ability to inhibit tyrosinase.

Materials and Methods

The non-protein fraction was subjected to GC-MS studies. The compounds identified from the GC-MS study were screened in silico for their ability to bind to tyrosinase enzyme. In vitro tyrosinase inhibitory assay of the non-protein extract was also studied.

Results and Discussion

Our results showed that the component, 1,3-bis(cinnamoyloxymethyl)adamantine showed stable binding with the tyrosinase enzyme. Molecular dynamics simulation of the complex of 1,3-bis(cinnamoyloxymethyl)adamantine and tyrosinase showed steady root mean square deviation values, Radius of gyration, root mean square fluctuation and solvent accessible surface area. Hydrogen bonding and van der Wals interaction were present between the ligand and the enzyme. In vitro tyrosinase assay showed that our extract had tyrosinase inhibitory effects.

Conclusion

The non-protein fraction from the sericin extract of Antheraea proylei J. can be further studied for their feasibility as a commercially available tyrosinase inhibitor.