荧光光谱法研究原花青素与牛血清白蛋白的相互作用

在pH=7.40的Tris-HCl缓冲体系中,采用荧光光谱技术研究了原花青素与牛血清白蛋白(BSA)的相互作用.根据295 K、303 K、310 K、315 K温度下的猝灭常数,表明原花青素对BSA的荧光猝灭为静态猝灭过程,由热力学参数焓变(△rHm)和熵变(△rSm)均大于零,推断出原花青素与BSA之间主要靠疏水作...     

荧光光谱法研究木犀草素与牛血清白蛋白的相互作用

在pH为7.40的Tris-HCl缓冲体系中,采用荧光光谱技术研究了木犀草素与牛血清白蛋白(BSA)的相互作用。根据测定292K、299K、311K温度下的猝灭常数,证实了木犀草素对BSA的荧光猝灭为静态猝灭过程,根据Frster非辐射能量转移理论计算出木犀草素与BSA间的结合距离r=2.75nm,由热力学参数焓变(△H)小于零和熵变(△S)大于零,推断出木犀草素与BSA之间主要靠静电引力相结合,生成自由能变(△G)为负值,表明木犀草素与BSA的作用过程是一个自发过程;同时,应用同步荧光光谱考察了木犀草素对BSA构象的影响。     

头孢拉定与血清白蛋白相互作用的光谱学研究

采用荧光和紫外吸收光谱法研究头孢拉定和牛血清白蛋白(BSA)的相互作用.研究发现,头孢柱定荧光猝灭牛血清白蛋白是由于形成了头孢拉定-牛血清白蛋白复合物.分别计算了不同温度下双分子猝灭常数kq和结合常数K.由热力学参数焓变(△H)、熵变(△S)和吉布斯自由能(△G),推断出头孢拉定与BSA的相互作用是一个疏水作用的自发过...     

水飞蓟素与牛血清白蛋白相互作用的荧光光谱研究

采用同步荧光光谱技术研究了pH=7.40的Tris-HCl缓冲体系中水飞蓟素与牛血清白蛋白(BSA)的相互作用以及水飞蓟素对BSA构象的影响.结果表明,水飞蓟素对BSA的荧光猝灭过程为静态猝灭,结合热力学参数△rH∞=-45.21 kJ·mol-1,△rSm=-61.61 J·K-1·mol-1;据此可以推断,水飞蓟素...     

荧光光谱法研究大豆甙元与牛血清白蛋白的相互作用

采用荧光光谱技术研究了大豆甙元与牛血清白蛋白(BSA)的相互作用.研究结果表明:290 K、303 K、310K、315 K温度下大豆甙元对BSA的猝灭速率常数Ksv随着温度升高逐渐降低,且均大于最大动态猝灭速率常数2×1010 L·mol -1·s-1,表明大豆甙元对BSA的荧光猝灭属静态猝灭过程.根据F(o)rst...     

非诺呋他林猝灭BSA荧光的机理研究及分析应用

在pH=7.4的Tris-HCl缓冲溶液中,非诺呋他林对牛血清白蛋白(BSA)的荧光有明显的猝灭作用,据此提出了以BSA为荧光试剂,利用其内源性荧光的变化来测定非诺呋他林的荧光分析新方法。在选定的实验条件下,非诺呋他林浓度在8.0×10-9~2.8×10-7 mol/L范围内与荧光猝灭值△F呈良好的线性关系(相关系数为0.9955),方法检出限为5.4×10-9 mol/L,相对标准偏差为0.86%(c=2.0×10-7 mol/L,n=5)。该方法用于样品中非诺呋他林的测定,结果满意。同时对体系的猝灭机理进行了研究。     

槲皮素-铝配合物的制备及其与BSA的结合作用

在甲醇溶液中合成了槲皮素-铝配合物(Que-Al),并用紫外-可见吸收光谱和红外光谱进行了表征;运用荧光光谱探讨了Que-Al与牛血清白蛋白(BSA)的相互作用;求得了结合常数KA和热力学参数△H、△G、和△S.结果表明,Que-Al对BSA具有荧光猝灭作用,其猝灭方式为动态猝灭;Que-Al与BSA之间的作用力主要为疏水作用力.     

盐酸苯肼与牛血清白蛋白相互作用的研究

用荧光光谱及紫外光谱研究了盐酸苯肼与牛血清白蛋白(BSA)的相互作用。实验结果表明,盐酸苯肼能导致BSA的内源荧光猝灭,猝灭机制为静态猝灭;根据热力学参数△H<0、△S<0,得出盐酸苯肼与BSA之间的主要作用力为氢键和范德华力。同步荧光的结果表明盐酸苯肼使BSA分子构象发生了改变,色氨酸和酪氨酸残基所处环境的疏水性降低。紫外光谱法进一步证明了其猝灭机制为静态猝灭。     

荧光光谱法研究左西孟旦与牛血清白蛋白的结合反应

用荧光光谱法、分光光度法研究了水溶液中左西孟旦与牛血清白蛋白(BSA)的相互结合反应。研究表明:左西孟旦对BSA的内源荧光有较强的猝灭作用且该猝灭作用属于静态荧光猝灭作用。得出了反应的结合常数(KA=1.48×106L/mol)和结合位点数(n=1.14)。根据Frster非辐射能量转移机理,求算了给体(BSA)与受体(左西孟旦)间距离r=2.9 nm和能量转移效率E=0.33。     

贝加因与牛血清白蛋白相互作用的分子光谱法研究

利用荧光光谱和吸收光谱研究了贝加因与牛血清白蛋白(BSA)的相互作用,由Van't Hoff方程计算了反应的热力学参数,并根据Stern-Volmer方程计算了不同温度下的结合位点和结合常数.结果表明,贝加因可静态猝灭BSA的内源荧光;二者相互作用的焓变和熵变均大于零,说明疏水作用力是二者之间的主要作用力.与此同时,贝...     

甘氨酸镧(Ⅲ)配合物与牛血清白蛋白的相互作用研究

红外光谱和X射线衍射分析表明甘氨酸与镧(Ⅲ)作用形成配合物。利用同步荧光光谱和荧光光谱探究了牛血清白蛋白(BSA)和甘氨酸镧(Ⅲ)配合物之间的相互作用。结果可知甘氨酸镧(Ⅲ)配合物与牛血清白蛋白的荧光猝灭为静态猝灭,根据双对数方程处理荧光猝灭数据得到了甘氨酸镧(Ⅲ)配合物与牛血清白蛋白在不同温度下的结合常数Kb和结合位点数n。热力学数据表明配合物与BSA作用主要是疏水作用力。利用同步荧光光谱法研究了甘氨酸镧(Ⅲ)配合物对于牛血清白蛋白的构象影响。     

荧光光谱法研究美托拉宗与牛血清白蛋白的相互作用

采用荧光光谱技术研究了在pH7.40的Tris-HCl缓冲介质中美托拉宗与BSA相互作用。实验发现,美托拉宗对BSA有较强的荧光猝灭作用,根据292K和311K时美托拉宗对BSA的荧光猝灭作用,利用Stern-Volmer方程及双倒数方程处理实验数据,表明美托拉宗对BSA的荧光猝灭作用属于动态猝灭过程,根据F rster非辐射能量转移理论计算出了美托拉宗与BSA间的结合距离r=2.77 nm,结合过程的热力学数据表明,二者主要靠疏水作用力结合;进一步采用同步荧光光谱探讨了美托拉宗对BSA构象的影响。     

氧氟沙星与脲诱导牛血清白蛋白结合的机制研究

摘要 利用荧光光谱和紫外光谱研究了脲（Urea）对牛血清白蛋白（BSA）结构的影响以及氧氟沙星（Oflxacin）与脲诱导的BSA结合的情况。结果显示：Urea诱导BSA变性历经两步、三态过程,且伴随中间态的形成。随着Urea浓度的增大,BSA荧光强度降低并先蓝移（344 nm～336 nm）,后又红移至350 nm。Urea浓度在4.6～5.2 mol/L范围时,Oflx对BSA中间态有强的猝灭作用（KQ=10.46×104 L/mol, Urea 4.8 mol/L）和较大的结合常数（KA=3.8807×105 L/mol, Urea 4.8 mol/L）,但是结合位点数小（n=0.76, Urea 5.0 mol/L）,能量传递效率低（E=0.3002, Urea 4.8 mol/L）。同步荧光光谱显示：Urea诱导BSA去折叠时,Trp-212残基微环境并未发生改变,而Tyr的最大荧光发射峰蓝移,Oflx的加入诱导Trp-212的微环境更具疏水性。Oflx加速了Urea对BSA的失活作用。     

灯盏花素与牛血清白蛋白相互作用的荧光光谱研究

采用荧光光谱法和紫外吸收光谱法研究了灯盏花素(BR)与牛血清白蛋白(BSA)的相互作用;利用热力学方程计算了295K和308K下的热力学参数ΔH、ΔG和ΔS,根据Stern-Volmer方程求出了猝灭常数和结合常数.结果表明,BR对BSA的荧光具有猝灭作用,其猝灭机制为动态-静态联合猝灭,BSA发射峰略有蓝移.BR与BSA之间的作用力主要为疏水作用.     

绞股蓝皂苷与牛血清白蛋白相互作用的荧光光谱研究

用荧光光谱技术研究了绞股蓝皂苷与牛血清白蛋白(BSA)在pH=7.40的Tris-HCl缓冲溶液中的相互作用;通过计算确定了绞股蓝皂苷与BSA的结合位点数和结合常数,利用热力学分析探讨了绞股蓝皂苷与BSA之间的结合方式;同时采用同步荧光技术考察了绞股蓝皂苷对BSA构象的影响.结果表明,绞股蓝皂苷对牛血清白蛋白的荧光猝灭过程为静态猝灭;二者主要靠疏水作用和静电引力结合.     

伊文思蓝作荧光探针研究牛血清白蛋白与氨苄青霉素之间的竞争反应

用伊文思蓝(Evans blue, EB)作荧光探针研究了氨苄青霉素(Ampicillin, A)对牛血清白蛋白(Bovine serum albumin, BSA)的竞争反应. 伊文思蓝与牛血清白蛋白作用, 使牛血清白蛋白荧光发生猝灭, 根据Stern-Volmer方程及荧光寿命研究了荧光猝灭的类型及机理. 结果表明, 猝灭类型为静态猝灭, 即伊文思蓝和牛血清白蛋白形成了一种稳定的复合物. 伊文思蓝与牛血清白蛋白的结合常数KBSA-EB=1.122×106 L/mol, 结合点数n=0.9935, 并确定了EB和BSA之间的热力学常数及作用力类型. 当加入氨苄青霉素后, 牛血清白蛋白的相对荧光强度恢复. 这表明氨苄青霉素与伊文思蓝对牛血清白蛋白发生了竞争反应. 探讨了该竞争反应的相关机理, 求出了伊文思蓝与氨苄青霉素的结合常数为KEB-A=7.131×105 L/mol.     

Analysis of binding interaction between pegylated puerarin and bovine serum albumin by spectroscopic methods and dynamic light scattering

The interaction between bovine serum albumin (BSA) and pegylated puerarin (Pur) in aqueous solution was investigated by UV-Vis spectroscopy, fluorescence spectroscopy and circular dichroism spectra (CD), as well as dynamic light scattering (DLS). The fluorescence of BSA was strongly quenched by the binding of pegylated Pur to BSA. The binding constants and the number of binding sites of mPEG(5000)-Pur with BSA were 2.67±0.12 and 1.37±0.05 folds larger after pegylating, which were calculated from the data obtained from fluorescence quenching experiments. The enthalpy change (ΔH) and entropy change (ΔS) were calculated to be 4.09 kJ mol(-1) and 20.01 J mol(-1) K(-1), respectively, according to Van't Hoff equation, indicating that the hydrophobic force plays a main role in the binding interaction between pegylated Pur and BSA. In addition, the negative sign for Gibbs free energy change (ΔG) implies that the interaction process is spontaneous. Moreover, the results of synchronous fluorescence and CD spectra demonstrated that the microenvironment and the secondary conformation of BSA were changed. Comparing with Pur, all our data collected indicated that pegylated Pur interacted with BSA in the same way as that of Pur, but docked into the hydrophobic pocket of BSA with more accessibility and stronger binding force. DLS measurements showed monomethoxy polyethylene glycol (mPEG) have an effect on BSA conformation, and revealed that changes in BSA size might be due to increases in binding constant and the absolute values of ΔG after Pur pegylation.     

Characterization of Interaction Between Raltitrexed and Bovine Serum Albumin by Optical Spectroscopic Techniques

The interaction of raltitrexed(RTX) with bovine serum albumin(BSA) was investigated by steady state/lifetime fluorescence spectroscopy and circular dichroism(CD) spectroscopy under the simulative physiological conditions. The results of fluorescence titration reveal that RTX could strongly quench the intrinsic fluorescence of BSA via a static quenching procedure. The obtained binding constant K_A of RTX with BSA was 478630 and 44259 L/mol at 298 and 310 K, respectively. According to van’t Hoff equation, the thermodynamic parameters ΔH, ΔG and ΔS were calculated, indicating that hydrophobic forces were the predominant intermolecular forces in stabilizing the complex. The binding process was a spontaneous process, in which Gibbs free energy change was negative. According to Förster’s non-radioactive energy transfer theory, the distance r between donor(BSA) and acceptor(RTX) was 3.82 nm, suggesting that the energy transfer from BSA to RTX occurred with high probability. Displacement experiment and the number of binding sites calculation confirmed that RTX could bind to the site-I of BSA. Furthermore, the effects of pH and some metal ions on the interaction of RTX with BSA were also investigated. The results of synchronous fluorescence and CD spectra show that the RTX-BSA binding induced conformational changes in BSA.     

Study of the interaction of indirubin with bovine serum albumin

This study examined the interaction of indirubin with bovine serum albumin (BSA) at three temperatures (286, 297, 308 K) at pH 7.40. In the presence of indirubin, the drug-BSA binding mode, binding constant and the protein structure changes in aqueous solution were determined by fluorescence quenching methods including Fourier transform infrared (FT-IR) spectroscopy and UV-Vis spectroscopy. The FT-IR change indicates that indirubin binds to BSA. The change in protein secondary structure accompanying ligand binding has been proved by fluorescence spectra data. The thermodynamic parameters, the enthalpy change (DeltaH), and the entropy change (DeltaS) calculated by the van't Hoff equation possess small negative (-2.744 kJ.mol(-1)) and positive values (112.756 J.mol(-1).K(-1)), respectively, which indicated that hydrophobic interactions play the main role in the binding of indirubin to BSA. Furthermore, the displacement experiment shows that indirubin can bind to the subdomain IIA and the distance between the tryptophan residues in BSA and indirubin bound to site I was estimated to be 2.24 nm according to F?ster's equation on the basis of fluorescence energy transfer.