Computational and biochemical evidence reveal cuminaldehyde as a potent tyrosinase inhibitor

Inhibition of enzymes has been a major drug target for curing diseases. Xanthine oxidase is involved in the production of uric acid. The enzyme has elevated levels of activity in various diseases like gout, cardiovascular diseases etc. Tyrosinase is a melanin producing enzyme. Increased levels of tyrosinase activity has been observed in a number of diseases like skin pigmentation disorders, melanoma tumors etc. Several investigations have not yielded inhibitors of these enzymes that have minimal side effects. Cuminaldehyde is a natural aldehyde which has been reported to be bioactive. The in-vitro enzyme activity assays for the enzymes xanthine oxidase and tyrosinase were done in absence and presence of cuminaldehyde. We docked cuminaldehyde against xanthine oxidase and tyrosinase proteins using Autodock 4.0 followed by molecular dynamics simulation. In-vitro enzyme activity assays showed that cuminaldehyde caused a better reduction of tyrosinase activity as compared to xanthine oxidase activity. Autodock analysis showed that cuminaldehyde bound favourably with both xanthine oxidase and tyrosinase. The simulation studies revealed that the tyrosinase protein took up an extended conformation when bound to cuminaldehyde and stable binding occurred between them. Cuminaldehyde cleared multiple drug filters and showed favourable ADMET properties. As such, cuminaldehyde can be further researched upon to validate its potential as an inhibitor of the tyrosinase protein.