用荧光光谱法研究了苏丹红Ⅱ与肌红蛋白(Mb)之间的相互作用. 实验结果表明,二者结合位点数近似为1,结合常数K=3.84×10~7 L/mol,有很强的相互作用. 用分子柔性对接技术模拟确定了它们之间的作用位点、作用力类型及相互作用能. 理论计算的结果表明,苏丹红Ⅱ和Mb相互作用的势能为-9 419.9 kJ/mol,静电能为-7 468.8 kJ/mol,范德华能为-1 951.0 kJ/mol. 苏丹红Ⅱ与Mb中His64残基形成氢键,苏丹红Ⅱ也能与疏水氨基酸残基,如能产生内源荧光的Phe33、Phe43、Phe106和Phe138等发生作用,这与苏丹红Ⅱ能使Mb荧光猝灭的实验结果一致.
The interactions between Sudan Ⅱ and Myoglobin(Mb) were investigated via fluorescence spectro-scopy. The experimental results suggest that there is strong interaction between Sudan Ⅱ and Mb. The binding site number n is about 1 and the binding constant, K, is 3. 84 × 10~7 L/mol. The position, type and energy of the interaction between Sudan Ⅱ and Mb were investigated by means of the flexible molecule docking technology. It was obtained from the theoretical calculation that the values of potential energy, electrostatic energy and van der waals energy of the interaction between Sudan Ⅱ and Mb are -9 419. 9, -7 468. 8, - 1 951. 0 kJ/mol, respectively. Sudan Ⅱ can form hydrogen bonds with His64 of Mb. In addition, Sudan Ⅱ can interact with Phe33, Phe43, Phe106 and Phe138 residues, which can produce fluorescence. Thus, the interaction can lead to the fluorescence quenching of Mb. This is in good agreement with the result of the fluorescence experiment.
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