共查询到19条相似文献,搜索用时 93 毫秒
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在模拟人体生理条件下,用荧光猝灭光谱、同步荧光光谱和紫外可见吸收光谱等,研究了25℃、31℃和38℃下甲硝唑(MET)与牛血清白蛋白(BSA)相互作用的热力学特征.采用Stern-Volmer方程、Lineweaver-Burk双倒数方程和热力学方程等分析实验数据,得到了相互作用常数KLB的平均值为3.116×104L·mol-1,热力学参数ΔHθ、ΔGθ和ΔSθ的平均值分别为-1.259 kJ·mol-1、-25.73 kJ·mol-1和80.47 J·K-1,结合位点数的平均值为1.086;实验表明,MET与BSA可结合形成具有一定结构的复合物,其荧光猝灭作用更符合静态猝灭作用特征,主要作用力可能是静电力.为研究MET的治病机制、生物学效应和生态环境效应等提供了重要信息. 相似文献
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研究药物和血浆中载体蛋白的相互作用对阐明药物在体内的转运、分布、代谢和药效等具有重要的意义。采用荧光光谱和紫外-可见吸收光谱法研究了不同温度下丹酚酸A(Sal A)与人血清白蛋白(HSA)的相互作用机理。研究结果表明,Sal A对HSA的内源荧光有明显的猝灭作用,猝灭过程为静态猝灭,并测定和计算得到不同温度下Sal A与HSA反应的结合常数、结合位点数。分析两者结合过程的热力学数据,表明Sal A和HSA的结合是一种自发的放热过程,且推测出Sal A与HSA之间的作用力为氢键和范德华力。 相似文献
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利用荧光光谱法研究缬沙坦与人血清白蛋白的作用机制。判断出缬沙坦对人血清白蛋白(HSA)体系的猝灭是由于生成复合物的静态猝灭,计算出在30℃缬沙坦与HSA相互作用的结合位点数和结合常数分别为n30℃=0.53和K30℃=761.8,37℃时缬沙坦与HSA相互作用的结合位点数和结合常数分别为n37℃=0.48和K37℃=374.8。此外,还得出了一些金属离子存在下的结合常数(KCa=3899.5,KCu=1081.4,KFe=1595.1,KZn=3833.6)。体系的热力学常数分别为ΔH=-24.9kJ/mol,ΔS30℃=38.2J.mol-1.K-1,ΔS37℃=34.5J.mol-1.K-1,由此得出缬沙坦与人血清白蛋白之间是以静电作用力相结合。由Frster非辐射能量转移理论计算出两者间的作用距离r=2.07nm。并利用同步荧光技术,考察了缬沙坦对蛋白质构象的影响。 相似文献
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首次依据有机磷的极性应用荧光光谱、紫外吸收光谱、同步荧光研究了在生理条件下(pH=7.4)乐果和对硫磷与鱼血清白蛋白(Fish Serum Albumin,FSA)的相互作用。推断FSA-乐果体系的作用力以氢键和范德华力为主、FSA-对硫磷体系的作用力以疏水作用力为主,FSA与乐果、对硫磷之间存在着非辐射能量转移。 相似文献
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应用荧光光谱法及紫外吸收光谱法研究了3-(2-羟乙基)-2-对甲苯胺基喹唑啉-4(3-H)-酮(HTQ)与牛血清白蛋白(BSA)的相互作用,计算了不同温度下的猝灭常数KSV、表观结合常数Kb以及主要的热力学参数ΔHθ、ΔGθ、ΔSθ等。结果表明,HTQ能强烈猝灭牛血清白蛋白的荧光强度,其荧光猝灭机理为动态猝灭;当HTQ与BSA以摩尔比1∶1结合形成复合物时,其结合过程主要是熵驱动,相互作用力主要为疏水作用力。根据F rster非辐射能量转移理论计算了给体(BSA)与受体(HTQ)之间的结合距离。 相似文献
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光谱法研究小分子药物与血清白蛋白的相互作用 总被引:1,自引:0,他引:1
本文采用荧光光谱法和紫外可见吸收光谱法,研究了盐酸多西环素(Doxycycline Hyclate)与牛血清白蛋白(Bovine Serum Albumin,BSA)相互作用的机理,探讨了温度对其反应的影响,并得到了不同温度下的结合常数KA,根据热力学常数确定了它们之间的主要作用力类型. 相似文献
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在模拟动物体生理条件下,用荧光光谱、三维荧光光谱、同步荧光光谱、紫外-可见吸收光谱等方法研究了在不同温度下,对硝基氯苯(PCNB)与牛血清白蛋白(BSA)结合反应的光谱行为。试验发现,PCNB对BSA有较强的荧光猝灭作用。用Stern-Volmer和Lineweaver-Burk方程及热力学方程分别处理试验数据,发现BSA与PCNB发生反应生成了新的复合物,属于静态荧光猝灭,得到了它们相互作用的生成常数KLB(1.557×104L/mol)、热力学参数(ΔHθ=-89.962kJ/mol,ΔSθ=-217.98J/K,ΔGθ=-23.93kJ/mol)和结合位点数(1.080)等。位点竞争实验结果显示PCNB与BSA的作用位置主要在BSA的SiteⅠ(Sub-domainⅡA)位。证明二者主要靠氢键和范德华力结合,同时用三维荧光光谱及同步荧光光谱法探讨了PCNB对BSA构象的影响,为研究PCNB的毒性和生物学效应提供了重要信息。 相似文献
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The mechanism of interaction between C.I. Direct Yellow 9 and human serum albumin was studied using spectroscopic methods including fluorescence spectra, UV–vis, Fourier transform infrared (FT-IR) and circular dichroism (CD). The quenching mechanism was investigated in terms of the association constants, number of binding sites and basic thermodynamic parameters. The distance between the human serum albumin donor and the acceptor dye was 3.64 nm as derived from fluorescence resonance energy transfer. Alteration of the secondary protein structure in the presence of the dye was confirmed by UV, FT-IR and CD spectroscopy. Molecular modeling revealed that a dye–protein complex was stabilized by hydrophobic forces and hydrogen bonding, via amino acid residues. 相似文献
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采用荧光光谱、紫外吸收光谱、动态光散射和Zeta电位法对比研究了十二烷基硫酸钠(SDS)和十二烷基三甲基溴化铵(DTAB)与牛血清白蛋白(BSA)的相互作用机理。结果表明:SDS和DTAB均能猝灭BSA内源荧光,298 K时的猝灭常数Ksv分别为2.64×104和304.21 L/mol。同步荧光光谱和三维荧光光谱显示SDS和DTAB对BSA的构象产生了影响。SDS对BSA荧光猝灭机理为动静联合猝灭机制;热力学计算表明,SDS与BSA的结合过程中,静电力起主导作用,并且能与BSA形成SDS/BSA超分子复合物;DTAB对BSA荧光猝灭机理为动态猝灭,作用力主要是疏水作用。SDS和DTAB与BSA的平均结合距离分别为2.77和4.73 nm。综合结合常数、粒径和Zeta电位等变化,在相同条件下具有较大电荷密度和较小体积极性头基的SDS与BSA具有更强的结合作用。 相似文献
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Peng Liu Yisi Liu Qisui Wang 《Journal of chemical technology and biotechnology (Oxford, Oxfordshire : 1986)》2012,87(12):1670-1675
BACKGROUND: Quantum dots (QDs) have attracted much attention in biological and medical applications. In particular, the interaction of QDs with bovine serum albumin (BSA) is crucial, and has been systematically investigated by various spectroscopic techniques under the physiological conditions. RESULTS: The effects of ionic strength and pH on the interaction of CdTe QDs with BSA were studied by changing NaCl concentration and pH in mixed solution and making fluorescence spectroscopic measurements. The Stern‐Volmer quenching constant (Ka) of different ionic strength and pH were calculated, and information on the structural features of BSA were discussed by means of circular dichroism (CD) spectrum. CONCLUSION: Both fluorescence (FL) and circular dichroism (CD) results indicated that hydrophobic and electrostatic interactions play a major role in the binding reaction, and the nature of quenching is static, resulting in forming QDs‐BSA complexes. Copyright © 2012 Society of Chemical Industry 相似文献
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Ximin Zhou Qing Yang Xiaoyun Xie Qin Hu Fengming Qi Zia Ur Rahman Xingguo Chen 《Dyes and Pigments》2012,92(3):1100-1107
In this study, the interaction between C.I. Acid Orange 7 (AO7) and human serum albumin (HSA) was firstly investigated using nuclear magnetic resonance (NMR) spectroscopy in combination with fluorescence quenching spectroscopy, three-dimensional fluorescence spectroscopy, UV-vis absorption spectroscopy, Fourier transform infrared (FT-IR) spectroscopy, circular dichroism (CD) spectroscopy and molecular modeling method in vitro. The results of NMR data confirmed that AO7 indeed interacted with HSA, and the hydrophobic portion of AO7 should be embedded to the hydrophobic pocket of HSA. The fluorescence quenching analysis revealed that AO7 can bind to HSA. The conformational change of HSA in the presence of AO7 was confirmed by synchronous fluorescence, three-dimensional fluorescence, UV-vis absorption, FT-IR and CD spectra. The binding distance between AO7 and tryptophan residue of HSA was calculated by the efficiency of fluorescence resonance energy transfer. Molecular modeling showed that hydrophobic force and hydrogen bonds were the major interaction between AO7 and HSA. 相似文献
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利用了荧光发射光谱,同步荧光光谱,紫外吸收光谱进行了检测,研究有机磷农药(草甘膦和马拉硫磷)与牛血清白蛋白的相互作用,实验结果表明了有机磷农药对牛血清白蛋白有着明显的荧光猝灭作用,且方式为静态猝灭(BSA荧光分子与猝灭剂有机磷农药之间通过弱的结合生成复合物,该复合物会使得荧光完全猝灭的现象)为主。通过实验得出有机磷与牛血清白蛋白的结合位点数(n),与结合常数(K0)。 相似文献
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Adsorption of proteins on solid surfaces is widely studied because of its importance in various biotechnological, medical, and technical applications, e.g., biosensors, cardiovascular implants, and chromatography. Adsorption thermodynamics has been studied on the microbeads of N,N′‐diethylaminoethyl (DEAE) Dextran anion exchanger for the human serum albumin (HSA) at 25, 30, 35, 40, and 45°C. As a result, some thermodynamic parameters like Freundlich constants, thermodynamic equilibrium constant (KD), standard free energy changes (ΔGassoc), standard entropy changes (ΔSassoc), and standard enthalpy change (ΔHassoc) have been evaluated. Using the linear Van't Hoff plot, ΔHassoc value of the system for the interaction of bovine serum albumin (BSA)‐adsorbed crosslinked DEAE dextran microbeads was determined as 20.650 kJ/mol. © 2006 Wiley Periodicals, Inc. J Appl Polym Sci 101: 3942–3947, 2006 相似文献