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.

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.

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.

Study of in vitro interaction between tetrabromobisphenol A and bovine serum albumin by fluorescence spectroscopy

2011 ◽  
Vol 30 (12) ◽  
pp. 2697-2700 ◽  
Author(s):  
Yingxin Wu ◽  
Yan Qian ◽  
Hao Cui ◽  
Xiaomin Lai ◽  
Xianchuan Xie ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Tetrabromobisphenol A ◽  
In Vitro Interaction

scholarly journals Ketoprofen-Based Ionic Liquids: Synthesis and Interactions with Bovine Serum Albumin

Molecules ◽  
2019 ◽  
Vol 25 (1) ◽  
pp. 90 ◽  
Author(s):  
Paula Ossowicz ◽  
Proletina Kardaleva ◽  
Maya Guncheva ◽  
Joanna Klebeko ◽  
Ewelina Świątek ◽  
...  
Keyword(s):  
Ionic Liquids ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Binding Constants ◽  
Protein Molecule ◽  
Binding Mode ◽  
Pharmaceutical Ingredients ◽  
System A ◽  
Static Mechanism

The development of ionic liquids based on active pharmaceutical ingredients (API-ILs) is a possible solution to some of the problems of solid and/or hydrophobic drugs such as low solubility and bioavailability, polymorphism and an alternative route of administration could be suggested as compared to the classical drug. Here, we report for the first time the synthesis and detailed characterization of a series of ILs containing a cation amino acid esters and anion ketoprofen (KETO-ILs). The affinity and the binding mode of the KETO-ILs to bovine serum albumin (BSA) were assessed using fluorescence spectroscopy. All compounds bind in a distance not longer than 6.14 nm to the BSA fluorophores. The estimated binding constants (KA) are in order of 105 L mol−1, which is indicative of strong drug or IL-BSA interactions. With respect to the ketoprofen-BSA system, a stronger affinity of the ILs containing l-LeuOEt, l-ValOBu, and l-ValOEt cation towards BSA is clearly seen. Fourier transformed infrared spectroscopy experiments have shown that all studied compounds induced a rearrangement of the protein molecule upon binding, which is consistent with the suggested static mechanism of BSA fluorescence quenching and formation of complexes between BSA and the drugs. All tested compounds were safe for macrophages.

scholarly journals Spectroscopic investigation of the interaction of bovine serum albumin with a novel cardiac agent V-09

2008 ◽  
Vol 22 (1) ◽  
pp. 43-50 ◽  
Author(s):  
Changyun Chen ◽  
Meihua Ma ◽  
Junqi Zhang ◽  
Lichen Wang ◽  
Bingren Xiang
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Average Distance ◽  
Cardiac Activity ◽  
Binding Constants ◽  
Entropy Change ◽  
Standard Entropy ◽  
Förster Energy Transfer ◽  
Standard Enthalpy Change

This study employs fluorescence spectroscopy to characterize the binding properties of a newly synthesized cardiac agent, V-09, on bovine serum albumin (BSA). This compound shows the highest cardiac activity in the whole series. The binding constantsKat 25°C and 37°C are obtained, the values are 7.12×104l mol–1, 4.66×104l mol–1, respectively. The standard enthalpy change (ΔH0) and the standard entropy change (ΔS0) are calculated to be –27.13 KJ mol–1and 1.854 J mol–1K–1, which indicated that hydrophobic forces play major role in the interaction between V-09 and BSA. The binding average distance between V-09 and BSA (2.57 nm) is obtained on the basis of the theory of Főrster energy transfer.

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