酪氨酸酶
化学
立体化学
对接(动物)
氢键
圆二色性
范德瓦尔斯力
动力学
酶
组合化学
有机化学
生物化学
分子
医学
护理部
物理
量子力学
作者
Qinfei Chen,Chao Shang,Mengqi Han,Chan Chen,Weikang Tang,Wenbin Liu
标识
DOI:10.1016/j.saa.2023.122644
摘要
Tyrosinase plays an important role in melanin synthesis. Inhibition against tyrosinase activity has been extensively focused on for pharmaceutical, food, cosmetic, and agricultural purpose. The inhibitory mechanism of scutellarein on tyrosinase was elaborated by coupling enzyme kinetics, multi-spectroscopy and computational simulation. Scutellarein remarkably inhibited tyrosinase activity with an IC50 value of 91 μM. Scutellarein reversibly inhibited tyrosinase in a competitive manner. Fluorescence quenching validated that interaction of scutellarein with tyrosinase occurred to form a complex with a binding constant of 6.11 × 104 M-1. Thermodynamic parameters suggested that scutellarein spontaneously bound with tyrosinase via hydrogen bond and van der Waals force. Three-dimensional fluorescence spectra and circular dichroism spectra revealed that scutellarein induced an obvious conformational change in tyrosinase. Molecular docking result predicted that scutellarein mainly bound with tyrosinase via Arg268 residue. Scutellarein effectively controlled the enzymatic browning of apple slices during storage. This research could give theoretical guiding significance in various application for tyrosinase inhibitors.
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