Inhibitory effect of phthalic Acid on tyrosinase: the mixed-type inhibition and docking simulations.

ABSTRACT: Tyrosinase inhibition studies are needed due to the medicinal applications such as hyperpigmentation. For probing effective inhibitors of tyrosinase, a combination of computational prediction and enzymatic assay via kinetics was important. We predicted the 3D structure of tyrosinase, used a docking algorithm to simulate binding between tyrosinase and phthalic acid (PA), and studied the reversible inhibition of tyrosinase by PA. PA inhibited tyrosinase in a mixed-type manner with a K(i) = 65.84 ± 1.10 mM. Measurements of intrinsic and ANS-binding fluorescences showed that PA induced changes in the active site structure via indirect binding. Simulation was successful (binding energies for Dock6.3 = -27.22 and AutoDock4.2 = -0.97 kcal/mol), suggesting that PA interacts with LEU73 residue that

SUBMITTER: Yin SJ 

PROVIDER: S-EPMC3102342 | biostudies-literature | 2011

REPOSITORIES: biostudies-literature