Akademik Veri Yönetim Sistemi
Journal of Molecular Structure, cilt.1355, 2026 (SCI-Expanded, Scopus)
In this study, the tyrosinase inhibitory activities of four newly synthesized compounds (3, 3a, 4, 4a) were evaluated using an in vitro tyrosinase inhibition assay. The inhibitory potency of each compound was determined by calculating their IC50 values, which ranged from 14.17 ± 4.34 to 79.21 ± 4.33 µM. Among the tested compounds, 4a exhibited the strongest tyrosinase inhibition (IC50 = 14.17 ± 4.34 µM), showing significantly higher potency than the standard inhibitor kojic acid (IC50 = 47.83 ± 5.72 µM, p < 0.0001). Kinetic analyses, performed using Lineweaver-Burk and secondary plots, revealed that both 4 and 4a act as competitive inhibitors, as indicated by constant Vmax values and increased Km values with increasing inhibitor concentrations. The binding constant (Ki) for both compounds was calculated to be 50.82 µM. These findings suggest that 4a, in particular, holds promise as a potent tyrosinase inhibitor, with potential applications in therapeutic targeting hyperpigmentation.