One-pot synthesis of biomimetic glutathione peroxidase with temperature responsive catalytic behaviors

Excessive reactive oxygen free radicals (ROS) are the main cause of various oxidative diseases. It is of great significance to develop antioxidant drugs that can intelligently regulate free radical concentrations. The biomimetic simulation of glutathione peroxidase (GPx) can provide an important theoretical basis for the development of antioxidant drugs. In order to explore a simple and efficient strategy for constructing biomimetic GPx, a microgel biomimetic GPx (PNTegel) with temperature responsive catalytic activity was prepared by a one-pot synthesis method. The PNTegel, with typical enzymatic catalytic characteristics, exhibited a maximum catalytic activity at 37 °C (υ ₀ = 11.51 mM min^-1). The investigation of the catalytic mechanism of PNTegel suggested that the binding of different hydrophobic substrates to PNTegel was altered by the change of hydrophobicity of poly(N-isopropylacrylamide) (PNIPAM) in the microgel scaffold of PNTegel during the temperature response process. The change of hydrophobicity was the main factor for regulating the catalytic activity of PNTegel, which resulted in a temperature responsive catalytic behavior of PNTegel. This new strategy for the simple and efficient construction of biomimetic GPx by a one-pot method provides important theoretical support for exploring the preparation of highly effective antioxidant drugs.