Inhibitory mechanism of two homoisoflavonoids from Ophiopogon japonicus on tyrosinase activity: insight from spectroscopic analysis and molecular docking.

ABSTRACT: The inhibition mechanism of two homoisoflavonoids from Ophiopogon japonicus including methylophiopogonanone A (MO-A) and methylophiopogonanone B (MO-B) on tyrosinase (Tyr) was studied by multiple spectroscopic techniques and molecular docking. The results showed that the two homoisoflavonoids both inhibited Tyr activity via a reversible mixed-inhibition, with a half inhibitory concentration (IC₅₀) of (10.87 ± 0.25) × 10^-5 and (18.76 ± 0.14) × 10^-5 mol L^-1, respectively. The fluorescence quenching and secondary structure change of Tyr caused by MO-A and B are mainly driven by hydrophobic interaction and hydrogen bonding. Molecular docking analysis indicated that phenylmalandioxin in MO-A and methoxy in MO-B could coordinate with a Cu

SUBMITTER: Wang L 

PROVIDER: S-EPMC9042378 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature