【作者】 庞月红；

【导师】 双少敏； Man Shing Wong；

【作者基本信息】 山西大学 ， 药物分析学， 2005， 硕士

【摘要】 第一章:本章简要概述了蛋白质的基本结构与性质、蛋白质与药物相互作用的研究进展、分子内电荷转移的研究以及阐述了蛋白质定量分析的研究现状。 第二章（一）:本章采用荧光光度法,紫外可见分光光度法研究了苄氟噻嗪与人血清蛋白的相互作用,以及在生理缓冲溶液中,温度、金属离子的存在对结合常数的影响,从热力学角度研究苄氟噻嗪与人血清蛋白的相互作用过程,得出了热力学参数△H和△S,△H=49.28KJ mol^-1>0,△S=258.83J mol^-1 K^-1>0,依据F（?）rster非辐射能量转移机理求出了两者的结合位置r=1.47。实验表明苄氟噻嗪通过静态猝灭过程对HSA的荧光有较强的猝灭作用,苄氟噻嗪与蛋白质的结合常数较大且温度对结合常数的影响不大。金属离子的存在使结合常数降低,一般降低30%-55%。苄氟噻嗪与人血清白蛋白亚结构域ⅡA之间发生了疏水的相互作用。 第二章（二）:本章采用荧光光度法,紫外可见分光光度法研究了不同酸度,不同温度下,降压利尿药氢氯噻嗪（Hydrochlorothiazide）与人血清白蛋白（HSA）间的相互作用。求得不同酸度下药物与人血清白蛋白相互作用的形成常数,讨论了微量金属离子对药物与血清白蛋白形成常数的影响,并根据热力学常数确定了该药物与血清白蛋白之间的作用力类型,在此基础上依据福斯特F（?）rster非辐射能量转移机理探讨了氢氯噻嗪与人血清白蛋白相互结合时其给体-受体间的距离和能量转移效率。 第三章:本文合成了新型硼酸化合物4-二苯氨基-4′-二苯基硼酸（DBBA）,并在室温条件下利用紫外可见吸收光谱和稳态荧光光谱法对该化合物在不同极性溶剂中的荧光量子产率、荧光寿命、偶极矩的差值等发光性质进行了表征。实验表明,化合物DBBA的荧光光谱有明显的溶剂效应。根据Lippert-Mataga方法计算出化合物DBBA在激发前后偶极矩的差值为5.0D。该化合物在不同极性溶剂中的荧光量子产率高,荧光寿命小,以及发射光谱红移,偶极距差值增大,从而进一步表明了该化合物具有分子内电荷转移的特性。 第四章:利用紫外可见吸收光谱和荧光光谱对新合成的化合物:对-二苯更多还原

【Abstract】 Chapter 1: The basic structure and property of protein had been introduced. The recent development of the interactions between protein and drug was described further. The property of intramolecular charge transfer and the development of determination of protein had also been reviewed. Chapter 2（1）: The interactions between bendroflumethiazide （BFTZ） and human serum albumin （HSA） have been studied by fluorescence and UV-Vis spectroscopy. Binding constants for drug attachment to the various binding sites of HSA have been measured at different temperatures in physiological buffer solution. The effect of metal ions on BFTZ interaction with HSA was also investigated. The thermodynamic parameters, ΔH and ΔS, have been calculated to be 49.28KJ mol^-1>0, and 258.83J mol^-1 K^-1>0, respectively. The distance between HSA and BFTZ, r, was determined to be 1.47 nm based on Forster’s non- radiative energy transfer theory. The experimental results reveal that BFTZ has a strong ability to quench the intrinsic fluorescence of HSA through a static quenching mechanism. Furthermore, the binding constants between BFTZ and HSA are remarkably independent of temperature, and decrease in the presence of various ions, usually by about 30%-55%. Hydrophobic interaction occurs between BFTZ and the sub-domain IIA of HSA.Chapter 2 （ II ） :We have studied the interaction of human serum albumin （HSA） with Hydrochorothiazide by fluorescence quenching method at different pH and temperature. The binding constants were obtained at different pH and temperature. We have also discussed the binding constants in the presence of various metal ions. According to the thermodynamic parameters the main sorts of binding force have also been obtained. The distance between HSA and Hydrochorothiazide and energy transfer efficient are determined according to the theory of energy transfer. Chapter 3: A new compound 4-（diphenylamino） biphenyl-4’-boronic acid更多还原