Unveiling tyrosinase inhibition: exploring secondary metabolites from <i>Fernandoa adenophylla</i> through biological screening and molecular docking

The current study investigated the tyrosinase inhibitory activity of compounds extracted from <i>Fernandoa adenophylla</i>, complemented by <i>in silico</i> analysis. Using methanolic extract and chromatography, several compounds were isolated and tested for their inhibitory effects against human and mushroom tyrosinase enzymes. The indanone derivative (Sample CC) emerged as the most potent inhibitor, demonstrating 96.32% inhibition with an IC50 of 6.2 ± 0.9 µg/mL against human tyrosinase and 91.3% inhibition with an IC50 of 1.8 ± 0.5 µg/mL against mushroom tyrosinase, surpassing the standard inhibitor, Kojic acid. <i>In silico</i> docking studies further supported these findings, revealing strong binding interactions between Sample CC and the active site of the tyrosinase, suggesting a robust inhibition mechanism. The analysis of interaction plots showed that the isolated compounds interact with key amino acid residues. These results highlight the potential of <i>F. adenophylla</i> compounds as natural tyrosinase inhibitors, offering promising alternatives for therapeutic and cosmetic applications.