采用分子动力学和分子力学相结合的方法 ,研究了一类 1,2 萘醌类抑制剂与酪氨酸蛋白磷酸酯酶PTP1B之间的相互作用模式 .计算得到的抑制剂和靶酶之间的相互作用模式显示范德华相互作用、疏水相互作用以及氢键作用是主要的作用模式 .计算结果还表明抑制剂和PTP1B的相互作用能ΔE越低 ,抑制剂活性越高 .通过计算各种能量对ΔE的贡献 ,以及对复合物结构参数的分析 ,发现抑制剂和受体之间疏水相互作用是造成抑制剂活性差别的主要原因 .这为设计其他非酸类抑制剂提供了信息 The interaction between a class of 1,2-naphthoquinone inhibitors and the tyrosine protein phosphatase PTP1B was studied by a combination of molecular dynamics and molecular mechanics.The calculated inhibitor and target enzyme Van der Waal’s interaction, hydrophobic interaction and hydrogen bonding are the main mode of action.The calculated results also show that the lower the interaction energy ΔE between inhibitor and PTP1B, the higher the activity of the inhibitor.Through the calculation of various energy pairs ΔE, as well as the analysis of the structural parameters of the complex, it was found that the hydrophobic interaction between the inhibitor and the receptor was responsible for the difference in the activity of the inhibitor, providing information for the design of other non-acid inhibitors