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.

Inhibition characteristics and mechanism of tyrosinase using five citrus flavonoids: A spectroscopic and molecular dynamics simulation study

“…Thus, both substrate and inhibitor could attach to the enzyme simultaneously in two different sites dependently, and the degree of inhibition affected by the change in the substrate concentration is dependent on the interaction between the two sites of substrate and inhibitor (Saboury, 2009). This same inhibition type has also been found in previous studies, in which epigallocatechin‐3‐gallate, gallocatechin gallate, homoisoflavonoids and trilobatin inhibited the diphenolase activity of tyrosinase (Song et al, 2021; Wang et al, 2021; Yu et al, 2021). These results suggest that the monophenolase and diphenolase activities of tyrosinase respond to one active site only during the three different stages of oxidation (Sánchez‐Ferrer et al, 1995).…”

“…The molecular dynamics method has previously been used to assess the structure and properties of reaction systems, including flavonoids and protein, as a supplement to experimental results (Wang et al, 2021). Root mean square deviation (RMSD) can evaluate the change in the stability of the complex structure following the binding of hesperetin or naringenin to tyrosinase (Song et al, 2021).…”

“…These results confirmed the result of the FTIR study, in which the H‐bond promoted the binding of tyrosinase with hesperetin or naringenin (Figure 3a). However, the binding sites of hesperetin and naringenin were different from those of the homoisoflavonoids of Ophiopogon japonicus , chrysin, naringin, quercetin and kaempferol (Farasat et al, 2020; Wang et al, 2021). Even within the same study, different molecules have been found to bind to tyrosine at different sites (Farasat et al, 2020), possibly due to either the structure of the ligand or the different solvent environments used in the molecular simulation.…”

“…of chloasma, senile spot, gestation spot and other human skin diseases (Wang et al, 2021). Moreover, tyrosinase's catalysis of melanin production is also involved in the browning of fruits and vegetables (Tinello & Lante, 2017).…”

Tetrabutylammonium bromide-based hydrophobic deep eutectic solvent for the extraction and separation of dihydromyricetin from vine tea and its inhibitory efficiency against xanthine oxidase

“…The detailed simulation steps were previously described. 28 Briefly, the Ff14SB field parameters were used for XO, the gaff general field parameters were for DMY–XO complex, and their AM1-BCC atomic charges were calculated using the ANTECHAMBER module. The DMY–XO molecular complex was loaded into the tleap module, and hydrogen atoms and antagonistic ions were automatically added to neutralize the charge.…”