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目的:研究了硫酸沙丁胺醇(salbutamol sulfate,SAS)与人血清白蛋白(human serum albumin,HSA)及人免疫球蛋白G(human Immunoglobulin G,HIg G)之间的相互作用。方法:在模拟生理条件下,采用分子模拟技术、紫外-可见吸收光谱法及圆二色谱法获得了HSA和HIg G结构改变的定性和定量依据。结果:根据分子对接技术所得数据可知:SAS与HSA之间的作用力主要是氢键、范德华力和静电作用;SAS与HIg G之间的作用力主要有氢键、π-正电荷相互作用和范德华力。紫外-可见吸收光谱实验结果表明当SAS加入到HSA和HIg G溶液中时,HSA和HIg G的二级结构会发生变化,并且SAS与HSA和HIg G之间的淬灭机制为静态淬灭;由圆二色谱所得到的定量数据可知SAS的加入使得HSA的α螺旋结构由47.92%减小到46.53%。与此同时,SAS的加入使得HIg G的二级结构产生变化。结论:分子模拟技术、紫外-可见吸收光谱法及圆二色谱法结合适合于研究SAS与HSA和HIg G之间的相互作用,具有简单快速,灵敏度高等优点。
Objective: To study the interaction between salbutamol sulfate (SAS) and human serum albumin (HSA) and human immunoglobulin G (HIg G). Methods: Under simulated physiological conditions, qualitative and quantitative basis of HSA and HIg G structure changes were obtained by molecular simulation, UV-Vis absorption spectroscopy and circular dichroism. Results: According to the data obtained from the molecular docking technology, the interaction between SAS and HSA is mainly hydrogen bond, van der Waal’s force and electrostatic interaction; the interaction between SAS and HIg G is mainly hydrogen bond, π-positive charge interaction and Van der Waals forces. The results of UV-vis absorption spectroscopy showed that the secondary structure of HSA and HIg G changed when SAS was added to HSA and HIg G solution, and the quenching mechanism between SAS and HSA and HIg G was static quenching. Quantitative data obtained by circular dichroism shows that the addition of SAS reduced the α-helix structure of HSA from 47.92% to 46.53%. In the meantime, the secondary structure of HIg G is changed by the addition of SAS. Conclusion: The molecular simulation techniques, UV-Vis absorption spectroscopy and circular dichroism are suitable for the study of the interaction between SAS and HSA and HIg G, with the advantages of simple and rapid, high sensitivity.