The Investigation of the Interaction between Daidzin and Bovine Serum Albumin by Fluorescence Spectroscopy

2014 ◽  
Vol 664 ◽  
pp. 402-409
Author(s):  
Qing Ming Wang ◽  
Jia Liu ◽  
Tian Xing Zhang ◽  
Feng Zhu ◽  
Xin Hui Tang
Keyword(s):  
Bovine Serum Albumin ◽  
Hydrogen Bonds ◽  
Fluorescence Quenching ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Binding Constant ◽  
Bovine Serum ◽  
Hydrophobic Interactions ◽  
Binding Constants ◽  
Apparent Binding Constant

We investigated the mutual interaction of daidzin with bovine serum albumin (BSA) by fluorescence spectroscopy. The results revealed that daidzin cause the fluorescence quenching of BSA through a static quenching procedure. The Stern-Volmer quenching constant (Ksv) were calculated at different temperature. The binding site (n), apparent binding constant (Ka) and corresponding thermodynamic parameters △Go, △Ho, △Sowere calculated and the van der Waals interaction, hydrogen bonds and hydrophobic interactions play an important role in stabilizing the complex. Besides, we also studied the effect of Cu2+, Ni2+, Mn2+and Co2+on the binding constants between daidzin and BSA, it is shows that the binding of BSA and daidzin is strengthened in the presence metal ions.

The Study on the Interaction Conditions of Water-Soluble Chitosan with Bovine Serum Albumin

2011 ◽  
Vol 347-353 ◽  
pp. 1281-1286
Author(s):  
Shan Shan Huang ◽  
Feng Zuo Qu ◽  
Tong Kuan Xu ◽  
Li Cui
Keyword(s):  
Bovine Serum Albumin ◽  
Fluorescence Quenching ◽  
Serum Albumin ◽  
Linear Relationship ◽  
Binding Constant ◽  
Bovine Serum ◽  
Fluorescence Spectra ◽  
Three Dimensional ◽  
Water Soluble ◽  
Visible Absorption

The interaction conditions between the water-soluble chitosans(WSC) and bovine serum albumin (BSA) was studied by Ultraviolet-visible absorption and fluorescence spectrometries. It was shown there was a good linear relationship between the absorbency A and the BSA concentration(0~1.5g/L) and WSC concentration (0~1.5 g/L). The fluorescence quenching of WSC to BSA was static quenching. When the temperature is 30°C, its binding constant Ka=5.35×104 L/mol, binding site n=1.05. The influence of WSC on the conformation of BSA was analyzed by sychronous fluorescence spectra and three-dimensional fluorescence spectrum.

scholarly journals Fluorescence Spectroscopy Study on the Interaction of Acetal Cleavable Anionic Surfactants and Bovine Serum Albumin

2014 ◽  
Vol 2014 ◽  
pp. 1-6 ◽  
Author(s):  
Xin Zhang ◽  
Jianhong Bian ◽  
Wenjie Zhai ◽  
Jing Dong ◽  
Huihui Liang ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Protein Separation ◽  
Anionic Surfactants ◽  
Binding Constants ◽  
Number Of Binding Sites ◽  
Hydrophobic Nature ◽  
Thermodynamic Relationship

The interactions between bovine serum albumin (BSA) and two cleavable anionic surfactants, sodium 3-[(2-nonyl-1,3-dioxolan-4-yl)methoxy]propane-1-sulfonate (SNPS) and sodium 3,3′-(2-nonyl-1,3-dioxane-5,5-diyl)bis(methylene)bis(oxy)dipropane-1-sulfonate (SNDPS), have been studied by means of fluorescence spectroscopy and thermodynamic analysis. The fluorescence of BSA is quenched via a static quenching mechanism with the addition of the surfactants. The binding constants of the surfactants and proteins have been measured, with KA(SNPS) = 8.71×104 M−1 and KA(SNDPS) = 7.08 × 104 M−1, respectively. The interaction between surfactants and BSA is mainly of hydrophobic nature, based on the number of binding sites, n[n(SNPS) = 1.57, n(SNDPS) = 1.47], and the thermodynamic relationship. These results suggest that SNPS and SNDPS could be effective protein denaturants for protein separation and analysis.

Study of the Interaction between Zinc Complex and Bovine Serum Albumin by Fluorescence Spectroscopy

2012 ◽  
Vol 554-556 ◽  
pp. 1678-1681 ◽  
Author(s):  
Yu Fen Liu ◽  
Hai Tao Xia ◽  
De Fu Rong
Keyword(s):  
Bovine Serum Albumin ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Binding Sites ◽  
Bovine Serum ◽  
Binding Constants ◽  
Gibbs Free Energy Change ◽  
Binding Reaction ◽  
Physiological Conditions ◽  
Number Of Binding Sites

The binding reaction of Zn(II) complex [Zn(C8H10N)2Cl2] with bovine serum albumin(BSA) was studied by fluorescence spectroscopy under the simulative physiological conditions. The intrinsic fluorescence of BSA could be quenched by Zn(II) complex. The quenching mechanism was suggested as static quenching according to the Stern–Volmer equation. The binding constants Kband the number of binding sites n were calculated. The Zn(II) complex exhibit good binding propensity to bovine serum albumin having relatively high binding constant values. The thermodynamic parameters indicate that the hydrogen bonds and van der Waals forces play a major role in BSA-Zn(II) complex association. The process of binding was spontaneous, in which Gibbs free energy change (ΔG) was negative.

scholarly journals Hydrophobic interactions of phenoxazine modulators with bovine serum albumin

2000 ◽  
Vol 112 (1) ◽  
pp. 51-61 ◽  
Author(s):  
H. N. Kalpana ◽  
B. C. Channu ◽  
Chhabil Dass ◽  
P. J. Houghton ◽  
K. N. Thimmaiah
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Hydrophobic Interactions

scholarly journals Investigating the Size-Dependent Binding of Pristine nC60 to Bovine Serum Albumin by Multi-Spectroscopic Techniques

Materials ◽  
2021 ◽  
Vol 14 (2) ◽  
pp. 298
Author(s):  
Shufang Liu ◽  
Shu’e Wang ◽  
Zhanzuo Liu
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Binding Constants ◽  
Inner Filter Effect ◽  
Spectroscopic Techniques ◽  
Size Distributions ◽  
Size Dependent ◽  
Filter Effect ◽  
Vis Spectroscopy

The morphology of nanomaterials may affect their interaction with biomacromolecules such as proteins. Previous work has studied the size-dependent binding of pristine nC60 to bovine/human serum albumin using the fluorometric method and found that the fluorescence inner filter effect might affect this interaction. However, if it is necessary to accurately calculate and obtain binding information, the fluorescence inner filter effect should not be ignored. This work aimed to further investigate the effect of the fluorescence inner filter on the interaction between pristine nC60 with different particle sizes (140–160, 120–140, 90–110, 50–70, and 30–50 nm) and bovine serum albumin for a more accurate comprehension of the binding of pristine nC60 to bovine serum albumin. The nC60 nanoparticles with different size distributions used in the experiments were obtained by the solvent displacement and centrifugation method. UV-Vis spectroscopy and fluorescence spectroscopy were used to study the binding of nC60 with different size distributions to bovine serum albumin (BSA) before and after eliminating the fluorescence inner filter effect. The results showed that the fluorescence inner filter effect had an influence on the interaction between nC60 and proteins to some extent, and still did not change the rule of the size-dependent binding of nC60 nanoparticles to BSA. Further studies on the binding parameters (binding constants and the number of binding sites) between them were performed, and the effect of the binding on BSA structures and conformation were also speculated.

Interaction between felodipine and bovine serum albumin: fluorescence quenching study

Luminescence ◽  
2009 ◽  
pp. n/a-n/a ◽  
Author(s):  
U. S. Mote ◽  
S. L. Bhattar ◽  
S. R. Patil ◽  
G. B. Kolekar
Keyword(s):  
Bovine Serum Albumin ◽  
Fluorescence Quenching ◽  
Serum Albumin ◽  
Bovine Serum
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