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利用紫外吸收光谱、荧光光谱结合分子模拟技术研究了在模拟生理条件下甲磺酸酚妥拉明(phentolamine mesylate,PM)与肌红蛋白(myoglobin,Mb)的作用机制.实验结果表明:药物小分子甲磺酸酚妥拉明与蛋白相互作用时结合位点数为1,表观结合常数KA为5.27×104L·mol-1.分子模拟结果表明:PM在Mb上的结合位点是site1活性口袋,两者通过疏水作用、亲水作用、氢键作用以及静电作用结合.PM与Mb中的氨基酸残基Trp,Tyr和Phe发生疏水相互作用,进而导致Mb的紫外吸收峰强度降低以及荧光的猝灭.它们之间负的ΔG值表明结合反应是热力学允许的。
The mechanism of action of phentolamine mesylate (ME) and myoglobin (Mb) under simulated physiological conditions was studied by ultraviolet absorption spectroscopy, fluorescence spectroscopy and molecular simulation techniques. The experimental results show that the drug is small The binding site of phentolamine mesylate and protein was 1 and the apparent binding constant KA was 5.27 × 104 L · mol -1. The molecular simulation results showed that the binding site of PM on Mb was site1 active pocket , Both of which are combined by hydrophobic interaction, hydrophilic interaction, hydrogen bonding interaction and electrostatic interaction.The interaction of PM with the amino acid residues Trp, Tyr and Phe in Mb leads to the decrease of the intensity of UV absorption peak of Mb and the quenching of fluorescence Off. The negative ΔG values between them indicate that the binding reaction is thermodynamically tolerable.