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机构地区:[1]吉林化工学院分析测试中心,吉林132022 [2]吉林化工学院化学与制药工程学院,吉林132022 [3]济南大学资源与环境学院,济南250022
出 处:《基因组学与应用生物学》2017年第10期3937-3942,共6页Genomics and Applied Biology
基 金:国家自然基金(21107029);吉林省教育厅(2014351;2014344);吉林市科技局(20166023)共同资助
摘 要:本研究在模拟生理条件(p H=7.404)下,用光谱法研究了HSO_3^-荧光探针(BCZ-3)与人血清白蛋白(HSA)之间的相互作用。结果表明,探针BCZ-3与HSA之间的猝灭机理主要是静态猝灭。由计算得到的热力学参数显示二者之间的作用力类型为范德华力和氢键。二者之间的结合距离经测算为3.35 nm。利用同步荧光光谱、CD光谱、紫外光谱以及三维荧光光谱研究表明,与探针BCZ-3的结合改变了HSA的构象。本研究为今后HSO_3^-荧光探针的设计提供了理论依据,也有助于进一步探讨其识别机制和生物学效应。In this study, we investigated the interaction between HSO3-- fluorescent molecular probe(BCZ-3) and human serum albumin(HSA) with spectroscopy in simulated physiological conditions(p H=7.404). The result showed that the quenching mechanism between probe BCZ-3 and HSA was mainly static quenching. The calculated thermodynamic parameters revealed that the type of acting force between them was Van der Waals forces and hydrogen bond. The binding distance of them was measured to be 3.35 nm. By researching with synchronous fluorescence, CD, ultraviolet and three-dimensional fluorescence spectrum, we discovered that combining with the BCZ-3 changed the conformation of HSA. This study could provide a theoretical basis on the design of HSO3^- fluorescent probe in future, and would also be helpful to the further study of its recognize mechanism and biological effect.
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