共查询到20条相似文献,搜索用时 109 毫秒
1.
2.
在pH=7.4的生理条件下,应用荧光光谱法研究了速灭威与牛血清白蛋白间相互作用。结果表明:速灭威对牛血清白蛋白的荧光有较强的猝灭作用,测定不同温度下的猝灭常数,证实了速灭威对牛血清白蛋白的荧光猝灭过程机理为静态猝灭。根据猝灭结果计算了不同温度下的结合位点数、结合常数。应用同步荧光光谱法探讨了速灭威对牛血清白蛋白构象的影响。依据f ster非辐射能量转移理论确定受体间的结合距离和能量转移效率。 相似文献
3.
4.
用荧光光谱和共振光散射光谱研究甲硝唑与牛血清白蛋白的相互作用 总被引:2,自引:0,他引:2
用荧光光谱和共振光散射光谱对甲硝唑与牛血清白蛋白的作用进行了对比研究, 测定了该反应的结合常数、结合位点数. 探讨了甲硝唑对牛血清白蛋白荧光和共振光散射猝灭的机理. 利用热力学参数确定了分子间的作用力性质;根据非辐射能量转换机制, 确定了甲硝唑-牛血清白蛋白间的结合距离. 采用同步荧光技术考察了甲硝唑对牛血清白蛋白构象的影响. 相似文献
5.
采用荧光光谱、紫外光谱对吡柔比星与牛血清白蛋白的相互作用进行了研究。结果表明,吡柔比星和牛血清白蛋白可形成基态配合物导致牛血清白蛋白的内源荧光猝灭,猝灭机理主要为静态猝灭和非辐射能量转移。通过计算获得了二者在不同温度下的结合常数及结合位点数。根据热力学参数判断吡柔比星与牛血清白蛋白之间的作用力主要为范德华力和氢键。根据Frster非辐射能量转移理论确定了吡柔比星和牛血清白蛋白的作用距离。研究了不同金属离子存在下对吡柔比星与牛血清白蛋白结合常数及结合位点数的影响。 相似文献
6.
氯霉素(CHL)和沙拉沙星(SLFX)均能够猝灭牛血清白蛋白(BSA)的荧光. 当两种药物共存时使BSA荧光进一步猝灭, 据此利用荧光光谱法研究了氟喹诺酮类药物SLFX与CHL间相互作用. 结果表明: 两种药物间存在拮抗作用, 使药物与蛋白的结合稳定性增加, 致使能够转运到作用部位产生药理效应的游离型药物含量减少, 造成药效降低; 药物对蛋白荧光的猝灭属于静态猝灭; 药物与蛋白结合位点数约为1. 根据Forster非辐射能量转移理论, 确定了药物与蛋白之间的结合距离r, 药物间拮抗作用的存在使r值降低, 结合距离减小. 同步荧光光谱研究表明, 药物间的拮抗作用对蛋白质构象产生影响, 使蛋白质分子伸展, 疏水性降低. 相似文献
7.
采用荧光光谱法和紫外-可见分光光度法研究了变色酸与牛血清白蛋白之间的相互作用。结果表明:变色酸对牛血清白蛋白有较强的荧光猝灭作用。根据Stern-Volmer方程得到了荧光猝灭常数,并判断由于与变色酸反应而导致牛血清白蛋白的荧光猝灭属于静态猝灭。采用Lang-muir单分子吸附模型计算了结合常数和结合位点数。从计算得到的热力学参数ΔH和ΔS推断了变色酸与血清白蛋白反应的作用力为氢键和范德华力。 相似文献
8.
9.
10.
荧光光谱法研究木犀草素、芹菜素或葛根素与牛血清白蛋白的相互作用机理 总被引:1,自引:0,他引:1
利用紫外可见光谱和荧光光谱法研究三种黄酮类药物木犀草素、芹菜素和葛根素与牛血清白蛋白(BSA)在不同温度下(292 K和311 K)的相互作用。结果表明:三种黄酮类药物与牛血清白蛋白形成复合物导致牛血清白蛋白荧光猝灭,试验数据采用Stern-Volmer拟合方程处理及双对数方程处理,进一步证明结合反应引起的荧光猝灭属于静态猝灭。采用位点结合模型公式、热力学公式和F rster非辐射能量转移理论计算了结合常数、结合位点数及作用力类型以及结合距离。 相似文献
11.
12.
Li D Wang Y Chen J Ji B 《Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy》2011,79(3):680-686
The binding of farrerol to bovine serum albumin (BSA) in aqueous solution was investigated by fluorescence quenching spectra, synchronous fluorescence spectra, circular dichroism (CD) and the three-dimensional (3D) fluorescence spectra at pH 7.40. The results of fluorescence titration indicated that farrerol could quench the intrinsic fluorescence of BSA in a static quenching way. The cause of showing upward curvy patterns in Stern-Volmer plots was analyzed. The binding sites number n and binding constant K using fluorescence quenching equation at 310 K were calculated. The binding distance and the energy transfer efficiency between farrerol and BSA were also obtained according to the theory of F?rster's non-radiation energy transfer. The effect of some metal ions on the binding constant of farrerol with BSA was also studied. The effect of farrerol on the conformation of BSA was analyzed using CD, synchronous fluorescence spectra and three-dimensional (3D) fluorescence spectra under experimental conditions. Furthermore, the fluorescence displacement experiments indicated that farrerol could bind to the site I of BSA. 相似文献
13.
Jayabharathi J Thanikachalam V Srinivasan N Perumal MV 《Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy》2011,84(1):233-237
Novel bioactive imidazole derivatives were synthesized and characterized by NMR spectra, mass and CHN analysis. The interaction between the imidazole derivative and bovine serum albumin (BSA) was investigated by fluorescence and UV-vis absorption spectroscopy. The fluorescence quenching of BSA by the imidazole derivatives may be due to the formation of imidazole-BSA complex. The fluorescence quenching mechanism of BSA by imidazole was analyzed and the binding constant has been calculated. The binding distance between imidazole and BSA was obtained based on Forester's non-radiation energy transfer (FRET). The effect of some common ions on the binding constant between imidazole and BSA was also examined. 相似文献
14.
15.
The interactions between bilirubin (BR) and bovine serum albumin (BSA) have been studied by fluorescence spectroscopy. The
association constant between BR and BSA was obtained by fluorescence enhancement titration. Furthermore, fluorescence quenching
was studied at different temperatures, and the binding constant was also determined by the method of fluorescence quenching.
The two methods yielded similar results. It indicated that the former method could be successfully applied to the determination
of BR. The results showed that the binding of BR to BSA induced conformational changes in BSA. Based on the theory of F?rster
energy transfer, the distance between BR and protein were calculated. According to the thermodynamic parameters, the main
binding force could be judged. The experimental results revealed that BSA and BR had strong interactions. The mechanism of
quenching belonged to static quenching and the main sort of binding force was van der Waals interactions and hydrogen bonds. 相似文献
16.
采用荧光光谱法和紫外光谱法研究了大黄酸铜配合物与牛血清白蛋白之间的相互作用.大黄酸铜配合物能显著猝灭牛血清白蛋白的内源荧光并以静态猝灭为主;计算了298 K和309 K温度下结合常数、结合位点,根据热力学参数判断大黄酸铜配合物与牛血清白蛋白之间具有较强的疏水作用力;依据F?rster的偶极-偶极非辐射能量转移理论,计算出大黄酸铜在蛋白质中结合位置与色氨酸残基间的距离为3.21 nm, 表明大黄酸铜的部分片段能够插入蛋白质分子内部;用同步荧光光谱和圆二色光谱技术探讨了大黄酸铜对牛血清白蛋白构象的影响. 相似文献
17.
18.
The interactions between potassium perfluorooctanesulfonate (PFOS) and bovine serum albumin (BSA) were studied by fluorescence spectroscopy. The association constants between PFOS and BSA were obtained by fluorescence enhancing and fluorescence quenching respectively. Furthermore, fluorescence quenching was studied at different temperatures, and the binding constant was also determined by the method of fluorescence quenching. According to the thermodynamic parameters, the main binding force could be judged. The experimental results revealed that BSA and PFOS had strong interactions. The mechanism of quenching belonged to dynamic quenching and the main sort of binding force was hydrophobic force. IR-spectra proved the interaction changed the conformation of BSA. 相似文献
19.
合成了白杨素磺酸钠和白杨素磺酸钙两种白杨素磺酸盐衍生物,并分别采用荧光光谱法研究了它们与牛血清白蛋白(BSA)的相互作用。结果表明:两种白杨素磺酸盐对BSA有较强的荧光猝灭作用,根据Stern-Volmer方程得到的荧光猝灭常数,可判断由于与白杨素磺酸盐反应而导致BSA的荧光猝灭均属于静态猝灭。采用位点结合模型公式和Frster非辐射能量转移理论计算了结合常数、结合位点数、结合距离。从计算得到的热力学参数焓变ΔH和熵变ΔS,推断了白杨素磺酸钠与BSA之间的作用力为静电引力,而白杨素磺酸钙与BSA之间的作用力为氢键和范德华力。并应用同步荧光技术研究了白杨素磺酸盐对BSA构象的影响。 相似文献
20.
Yu X Lu S Yang Y Li X Yi P 《Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy》2011,83(1):609-613
The fluorescence and ultraviolet spectroscopies were explored to study the interaction between N-confused porphyrins-edaravone diad (NCP-EDA) and bovine serum albumin (BSA) under simulative physiological condition at different temperatures. The experimental results show that the fluorescence quenching mechanism between NCP-EDA and BSA is a combined quenching (dynamic and static quenching). The binding constants, binding sites and the corresponding thermodynamic parameters (ΔG, ΔH, and ΔS) of the interaction system were calculated at different temperatures. According to F?rster non-radiation energy transfer theory, the binding distance between NCP-EDA and BSA was calculated to be 3.63 nm. In addition, the effect of NCP-EDA on the conformation of BSA was analyzed using synchronous fluorescence spectroscopy. 相似文献