scholarly journals Binding Constants of Substituted Benzoic Acids with Bovine Serum Albumin

2020 ◽  
Vol 13 (2) ◽  
pp. 30 ◽  
Author(s):  
Diliara Khaibrakhmanova ◽  
Alena Nikiforova ◽  
Igor Sedov
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Equilibrium Constants ◽  
Binding Constants ◽  
Quantitative Structure Activity Relationship ◽  
Drug Candidates ◽  
Hammett Constants ◽  
Qsar Models ◽  
Substituted Benzoic Acids

Experimental data on the affinity of various substances to albumin are essential for the development of empirical models to predict plasma binding of drug candidates. Binding of 24 substituted benzoic acid anions to bovine serum albumin was studied using spectrofluorimetric titration. The equilibrium constants of binding at 298 K were determined according to 1:1 complex formation model. The relationships between the ligand structure and albumin affinity are analyzed. The binding constant values for m- and p-monosubstituted acids show a good correlation with the Hammett constants of substituents. Two- and three-parameter quantitative structure–activity relationship (QSAR) models with theoretical molecular descriptors are able to satisfactorily describe the obtained values for the whole set of acids. It is shown that the electron-density distribution in the aromatic ring exerts crucial influence on the albumin affinity.

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.

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.

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.

Complexes of bovine serum albumin with water-soluble Cu and Co containing cationic meso-tetra(4-N-oxyethylpyridyl)-porphyrins

2007 ◽  
Vol 11 (07) ◽  
pp. 475-480 ◽  
Author(s):  
Nelli H. Karapetyan ◽  
Lusine R. Aloyan ◽  
Robert K. Ghazaryan ◽  
Yevgeni Mamasakhlisov
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Visible Region ◽  
Binding Constants ◽  
Water Soluble ◽  
Albumin Binding ◽  
Binding Isotherms ◽  
Bovine Serum Albumin Binding ◽  
Scatchard Plots

Bovine serum albumin complexes with water-soluble cationic porphyrins, Cu - and Co-meso-tetra(4- N -hydroxyethylpyridyl)porphyrins ( CuT4OEPyP , CoT4OEPyP ), and their 3- N -analogs, meso-tetra(3- N -hydroxyethylpyridyl)porphyrins ( CuT3OEPyP , CoT3OEPyP ), have been investigated. The porphyrin-bovine serum albumin binding was monitored by the absorption in the visible region at 400-460 nm. The stoichiometry of binding and the binding constants of the porphyrins to bovine serum albumin were determined using binding isotherms and Scatchard plots. The K b values obtained for these porphyrin- bovine serum albumin complexes are 1.7 × 105 M −1, 3.2 × 105 M −1, 1.4 × 105 M −1 and 3 × 105 M −1 respectively. Binding constants are sensitive to pH and ionic strength of the solution.

scholarly journals Deuteroporphyrin-albumin binding equilibrium. The effects of porphyrin self-aggregation studied for the human and the bovine proteins

1985 ◽  
Vol 229 (1) ◽  
pp. 197-203 ◽  
Author(s):  
M Rotenberg ◽  
R Margalit
Keyword(s):  
Human Serum Albumin ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Bovine Serum ◽  
Binding Constants ◽  
Protein Molecule ◽  
Competitive Model ◽  
Phosphate Buffered Saline ◽  
Self Aggregation

The binding equilibrium of deuteroporphyrin IX to human serum albumin and to bovine serum albumin was studied, by monitoring protein-induced changes in the porphyrin fluorescence and taking into consideration the self-aggregation of the porphyrin. To have control over the latter, the range of porphyrin concentrations was chosen to maker dimers (non-covalent) the dominant aggregate. Each protein was found to have one high-affinity site for deuteroporphyrin IX monomers, the magnitudes of the equilibrium binding constants (25 degrees C, neutral pH, phosphate-buffered saline) being 4.5 (+/- 1.5) X 10(7) M-1 and 1.7 (+/- 0.2) X 10(6) M-1 for human serum albumin and for bovine serum albumin respectively. Deuteroporphyrin IX dimers were found to bind directly to the protein, each protein binding one dimer, with high affinity. Two models are proposed for the protein-binding of porphyrin monomers and dimers in a porphyrin system having both species: a competitive model, where each protein molecule has only one binding site, which can be occupied by either a monomer or a dimer; a non-competitive model, where each protein molecule has two binding sites, one for monomers and one for dimers. On testing the fit of the data to the models, an argument can be made to favour the non-competitive model, the equilibrium binding constants of the dimers, for the non-competitive model (25 degrees C, neutral pH, phosphate-buffered saline), being: 8.0 (+/- 1.8) X 10(8) M-1 and 1.2 (+/- 0.6) X 10(7) M-1 for human serum albumin and bovine serum albumin respectively.

scholarly journals Comparative Studies on the Interaction of Cochinchinenin A and Loureirin B with Bovine Serum Albumin

2013 ◽  
Vol 2013 ◽  
pp. 1-9 ◽  
Author(s):  
Tianming Yang ◽  
Hao Zhang ◽  
Haiyan Fu ◽  
Yuanbin She ◽  
Can Huang ◽  
...  
Keyword(s):  
Circular Dichroism ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Binding Constants ◽  
Static Quenching ◽  
Spectrophotometric Methods ◽  
Quenching Efficiency ◽  
Circular Dichroïsm ◽  
Loureirin B

This paper describes the simple, sensitive, and effective spectrophotometric methods based on ultraviolet, fluorescence and circular dichroism for revealing the interactional mechanism of Cochinchinenin A (CA) and Loureirin B (LB) with bovine serum albumin (BSA). Under simulated physiological conditions, it was demonstrated that the fluorescence quenching mechanisms between CA (or LB) and BSA as a static quenching mode, or a combined quenching (dynamic and static quenching) mode were related to concentration level of CA (or LB). The binding distance (rCA,rLB) and the quenching efficiency (KSV), especially for the binding constants value of ligands to BSA, were affected by the methoxyl group at position 4 at different temperatures. The corresponding thermodynamic parameters were also obtained and indicated that electrostatic forces play a major role in the formation of the LB-BSA complex, but probably a combined force for CA-BSA complex. Furthermore, synchronous fluorescence spectroscopy and circular dichroism spectra demonstrated that the secondary structures of BSA were changed to varying degrees by the binding of CA (or LB).

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