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Bao-Sheng Liu Chun-Li Xue Jing Wang Chao Yang Yun-Kai Lv 《Monatshefte für Chemie / Chemical Monthly》2012,37(3):203-209
Abstract
Ponceau S (PS) can quench the fluorescence of bovine serum albumin (BSA) in aqueous solution of pH 7.40. The static fluorescence-quenching process between BSA and PS was confirmed and the binding constant, the number of binding sites, and thermodynamic data for the interaction between BSA and PS were obtained. The results showed that the number of binding sites was 1 and that electrostatic attraction was important in the binding of BSA to PS. On the basis of the theory of F?rster resonance energy transfer, the binding distance (r < 7 nm) between PS and BSA was obtained. Site marker competitive experiments indicated that binding of PS to BSA primarily occurred in sub-domain IIA (site I). There was no obvious fluorescence intensity change on combining BSA and gentamicin (GM), so the conjugation reaction between BSA and GM cannot be studied by spectroscopy. It was observed that when GM was added to the BSA–PS system, the relative fluorescence intensity of the system recovered gradually with increasing concentration of GM, which showed there was a conjugation reaction between GM and BSA and that binding of GM to BSA primarily occurred in sub-domain IIA (site I). 相似文献2.
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Hou X Tong X Dong W Dong C Shuang S 《Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy》2007,66(3):552-556
A new synchronous fluorescence scan analysis was developed for the determination of HSA with high sensitivity with a triphenylmethane acid dye methyl blue as a fluorescence probe. When Deltalambda=140 nm, the synchronous fluorescence peak of methyl blue is located at 323 nm and the synchronous fluorescence intensity of the methyl blue is significantly increased in the presence of trace HSA due to the complex formed between methyl blue and HSA at pH 4.1. Under optimal conditions, the calibration graphs are linear over the range 0.03-266.0 and 266.0-665.0 microg mL(-1) for human serum albumin (HSA). Limit of determination were 0.03 microg mL(-1) for HSA. In the detection of HSA in human serum samples, this method gave values close the clinical data got from hospital. 相似文献
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Yu X Liu R Yi R Yang F Huang H Chen J Ji D Yang Y Li X Yi P 《Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy》2011,78(4):1329-1335
The fluorescence and ultraviolet spectroscopy were explored to study the interaction between N-confused porphyrins (NCP) and bovine serum albumin (BSA) under imitated physiological condition. The experimental results indicated that the fluorescence quenching mechanism between BSA and NCP was static quenching procedure at low NCP concentration at 293 and 305 K or a combined quenching (static and dynamic) procedure at higher NCP concentration at 305 K. The binding constants, binding sites and the corresponding thermodynamic parameters ΔH, ΔS, and ΔG were calculated at different temperatures. The comparison of binding potency of the three NCP to BSA showed that the substituting groups in benzene ring could enhance the binding affinity. From the thermodynamic parameters, we concluded that the action force was mainly hydrophobic interaction. The binding distances between NCP and BSA were calculated using F?rster non-radiation energy transfer theory. In addition, the effect of NCP on the conformation of BSA was analyzed using synchronous fluorescence spectroscopy. 相似文献
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金属卟啉白蛋白结合体模拟SOD酶性能研究 总被引:1,自引:0,他引:1
将两类水难溶性金属卟啉(MP),meso-四苯基卟啉金属配合物(MTPP,M=ZnII,CoII)和meso-四(p-羟基苯基)卟啉金属配合物(MTpHPP,M=ZnII,CoII)分别与牛血清白蛋白(BSA)结合,制得水溶性金属卟啉白蛋白结合体(MP@BSA).采用UV-vis光谱、聚丙烯酰胺凝胶电泳(PAGE)、圆二色谱进行了表征与分析,发现金属卟啉的水溶性和稳定性得到大幅度提高.采用NBT光还原法测定了MP@BSA结合体清除超氧阴离子自由基(O2·-)的能力,发现结合体MP@BSA具有清除O2·-的性能,与小分子金属卟啉相比,结合体的抗O2·-性能提高了一个数量级.MP@BSA抗氧化活性分别是VC和BSA的600倍和40倍.其中,羟基取代金属卟啉结合体表现出更强的清除O2·-的活性,CoTpHPP@BSA的EC50为1.5μmol/L,对天然Cu,Zn-SOD的模拟度为2.73%.最后提出了生物高分子结合体清除O2·-的可能机理. 相似文献
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This work attempts to calculate the binding-site number using fluorescence spectroscopic method with bovine serum albumin
(BSA) and Indo-1 as protein and ligand models, respectively. The method for calculating the binding-site number in BSA for
Indo-1 was developed based on the relationships between changes in Indo-1 fluorescence intensity and the analytical concentration
of BSA. The interaction between BSA with Indo-1 was investigated comprehensively using fluorescence techniques as well as
fluorescence resonance energy transfer, and the thermodynamic parameters were calculated according to the effect of enthalpy
on temperature. Three binding sites in BSA for Indo-1 were revealed, and the distances from Trp212 in BSA to the three binding
sites were 2.93, 2.57 and 2.40 nm, respectively. It was also proven that Indo-1 embedded into the three hydrophobic cavities
of BSA by hydrophobic association. This paper provides a reference on calculating the binding-site number in proteins for
ligands and studying their interactions by fluorescence spectroscopic methods. In fluorescent quenching experiments, fluorescence
changes were automatically recorded in real time by combining the Microlab 500 Series Dispenser and PTI fluorescence apparatus.
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Translated from Chemical Journal of Chinese Universities, 2007, 28(2): 227–233 [译自: 高等学校化学学报] 相似文献
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Investigation of the association behaviors between biliverdin and bovine serum albumin by fluorescence spectroscopy 总被引:2,自引:0,他引:2
The interaction between biliverdin and bovine serum albumin (BSA) has been studied by steady fluorescence spectroscopy, synchronous fluorescence and resonance light scanning spectra. The binding of biliverdin to BSA quenches the tryptophan residue fluorescence and the results show that both static and dynamic quenching occur together with complex formation. The binding constant and binding sites of biliverdin to BSA at pH 7.1 are calculated to be 3.33 × 108 L/mol and 1.54, respectively, according to the double logarithm regression curve. In addition, the distance between the biliverdin and BSA is estimated to be 1.25 nm using Föster's equation on the basis of the fluorescence energy transfer. Furthermore the synchronous fluorescence spectra show that the microenvironment of the tryptophan residues has not obvious changes, which obeys the phase distribution model. Finally, the thermodynamic data show that biliverdin molecules enter the hydrophobic cavity of BSA via hydrophobic interaction. 相似文献
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由于半导体纳米晶体独特的物理和化学特性,具有优良的光谱特征和光化学稳定性,其作为荧光生物探针,在生物学、医学方面的学术价值和良好的发展前景正引起科学工作者的广泛关注[1~3]. 相似文献
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Yan-Jun Hu Yi Liu Li-Xia Zhang Ru-Ming Zhao Song-Sheng Qu 《Journal of Molecular Structure》2005,750(1-3):174-178
We investigated the interaction between colchicine and bovine serum albumin (BSA) by fluorescence and UV–Vis absorption spectroscopy. In the mechanism discussion, it was proved that the fluorescence quenching of BSA by colchicine is a result of the formation of colchicine–BSA complex; van der Waals interactions and hydrogen bonds play a major role in stabilizing the complex. The modified Stern–Volmer quenching constant Ka and corresponding thermodynamic parameters ΔH, ΔG, ΔS at different temperatures were calculated. The distance r between donor (BSA) and acceptor (colchicine) was obtained according to fluorescence resonance energy transfer (FRET). 相似文献