In this study, 5-methoxy-2-mercaptobenzimidazole (5-M-2-MB) was confirmed as an efficient tyrosinase inhibitor by methods of enzyme kinetic, fluorescence quenching, ANS-binding, thermodynamics, energy transfer, and molecular docking in combination. The results proved that 5-M-2-MB significantly inhibited the tyrosinase (IC₅₀ = 60 ± 2 nM) in a reversible and competitive way with the K_i value of 80 ± 1 nM. It quenched the intrinsic fluorescence of tyrosinase through a static mechanism, and caused conformational change of the enzyme by increasing the hydrophobic region. Moreover, this compound could bind to tyrosinase and form 5-M-2-MB-tyrosinase complex by hydrogen bond and hydrophobic interaction. The interactions were generated between 5-M-2-MB and specific amino acid residues (Trp-358, Thr-308, Glu-356, and Asp-357) located on the A chain of tyrosinase. Therefore, this study would offer a theoretical foundation for developing the new tyrosinase inhibitor.

在这项研究中，通过酶动力学，荧光猝灭，ANS结合，热力学，能量转移和分子对接相结合的方法，证实了5-甲氧基-2-巯基苯并咪唑（5-M-2-MB）是一种有效的酪氨酸酶抑制剂。 。结果证明5-M-2-MB 与K _i以可逆和竞争的方式显着抑制酪氨酸酶（IC ₅₀ = 60±2 nM）。值为80±1 nM。它通过静态机制淬灭了酪氨酸酶的内在荧光，并通过增加疏水区域引起了酶的构象变化。此外，该化合物可与酪氨酸酶结合并通过氢键和疏水相互作用形成5-M-2-MB-酪氨酸酶复合物。相互作用是在5-M-2-MB与位于酪氨酸酶A链上的特定氨基酸残基（Trp-358，Thr-308，Glu-356和Asp-357）之间产生的。因此，该研究将为开发新型酪氨酸酶抑制剂提供理论依据。