scholarly journals Interaction of Avelox with Bovine Serum Albumin and Effect of the Coexistent Drugs on the Reaction

2012 ◽  
Vol 2012 ◽  
pp. 1-8 ◽  
Author(s):  
Baosheng Liu ◽  
Chao Yang ◽  
Xiaona Yan ◽  
Jing Wang ◽  
Yunkai Lv
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Binding Site ◽  
Bovine Serum ◽  
Electrostatic Force ◽  
Binding Constants ◽  
Amino Acid Residues ◽  
Synchronous Fluorescence Spectra ◽  
Different Temperatures ◽  
Order Of Magnitude

The interaction between Avelox and bovine serum albumin (BSA) was investigated at different temperatures by fluorescence spectroscopy. Results showed that Avelox could quench the intrinsic fluorescence of BSA strongly, and the quenching mechanism was a static quenching process with Förester spectroscopy energy transfer. The electrostatic force played an important role on the conjugation reaction between BSA and Avelox. The order of magnitude of binding constants (Ka) was 104, and the number of binding site (n) in the binary system was approximately equal to 1. The binding distance (r) was less than 3 nm and the primary binding site for Avelox was located in subdomain IIA of BSA. Synchronous fluorescence spectra clearly revealed that the microenvironment of amino acid residues and the conformation of BSA were changed during the binding reaction. In addition, the effect of some antibiotics on the binding constant of Avelox with BSA was also studied.

Interaction of Nitroglycerin with Bovine Serum Albumin and the Influence of Metal Ions on the Binding

2020 ◽  
Vol 42 (2) ◽  
pp. 180-180
Author(s):  
Chengman Bao Chengman Bao ◽  
Jialian Wang Jialian Wang ◽  
Xuehong Tong Xuehong Tong ◽  
Chunli Zhang Chunli Zhang ◽  
Xinhui Tang Xinhui Tang
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Metal Ions ◽  
Bovine Serum ◽  
Binding Constants ◽  
Entropy Change ◽  
Quenching Rate ◽  
Different Temperatures ◽  
Quenching Rate Constant ◽  
Bimolecular Quenching

The effect of Cu2+, Ca2+, Mg2+and Zn2+ on the interaction between nitroglycerin and bovine serum albumin was investigated. The bimolecular quenching rate constant, the Stern-Volmer quenching constant, the binding constants and the number of binding sites were calculated in the absence and presence of Cu2+, Ca2+, Mg2+and Zn2+. The quenching constants of nitroglycerin to bovine serum albumin were increased in the presence of metal ions. Static quenching mechanism was also confirmed. The binding constants of nitroglycerin to bovine serum albumin were influenced by different metal ions. The enthalpy change, free energy chang, entropy change and the distance between the donor and the acceptor at different temperatures were calculated. The results indicated that energy transfer from bovine serum albumin to nitroglycerin occurs with high probability.

Quenching and binding mechanism of the intrinsic fluorescence of bovine serum albumin by 5-phenyl-10,15,20-tri-(4-pyridyl)-porphyrin

2009 ◽  
Vol 13 (08n09) ◽  
pp. 933-938
Author(s):  
Xin Chen ◽  
Yanyan Cai ◽  
Yanfang Zhao ◽  
Hongmin Ma ◽  
Dan Wu ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Electrostatic Force ◽  
Interaction Mechanism ◽  
Binding Constants ◽  
Theoretical Data ◽  
Radiation Energy ◽  
Binding Interaction

The binding interaction mechanism between 5-phenyl-10,15,20-tri-(4-pyridyl)-porphyrin (TriPyP) and bovine serum albumin (BSA) was investigated by the fluorescence method and presented in this paper. Based on the mechanism of fluorescence quenching of BSA caused by TriPyP, the binding constants between TriPyP and BSA were measured at different temperatures by fluorescence spectroscopy at pH 7.40. As the binding constants decreased with increasing temperature, the type of quenching between TriPyP and BSA was determined as static quenching. Based on the Förster theory of non-radiation energy transfer, the binding distance and energy transfer efficiency at 25 °C between TriPyP (acceptor of energy) and BSA (donor of energy) were obtained. The results confirmed that the interaction was similar to non-radiation energy transfer. According to the thermodynamic parameters, the main type of binding force between TriPyP and BSA could be deduced as electrostatic force. Using synchronous fluorescence spectra, the effect of TriPyP on conformation of BSA was studied, and the hydrophobicity in microenvironment was developed by TriPyP. All these experimental results and theoretical data clarified that TriPyP could bind to BSA and be effectively transported in the human body, which could be a useful guideline for further drug design.

scholarly journals Determining the degree of denaturation of bovine serum albumin using a new UV analysis technique

2021 ◽  
Vol 3 (1) ◽  
pp. 173-176
Author(s):  
Pooya Afaghi ◽  
◽  
Michael Anthony Lapolla ◽  
Khashayar Ghandi ◽  
◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Conformational Changes ◽  
Bovine Serum ◽  
Protein A ◽  
Amino Acid Residues ◽  
Analytical Technique ◽  
Analysis Technique ◽  
Different Temperatures ◽  
Denaturation Of Proteins

There is a lack of fast and inexpensive analysis methods to study the conformational changes and the degree of denaturation of proteins quantitatively. As such, a novel analytical technique is developed based on the ultraviolet-visible (UV-Vis) absorption spectrum of proteins, and a mathematical modeling of the results. The phenomenon behind this technique is the shift of the absorption peak of amino acid residues of BSA such as tyrosine, phenylalanine, and tryptophan as the protein unfolds and these residues are exposed to the solvent. However, the portion of the peak that is shifted is miniscule and it can be enhanced by using the proposed technique in this paper. As an example, we also show how this technique was applied for evaluating the temperature effects on thermal denaturation of bovine serum albumin (BSA) protein. A degree of denaturation curve as a function of time was obtained at three different temperatures using this technique. The results are reproducible and consistent with those reported in the literature. This technique is especially recommended for analyses where several tests are needed quickly, and the amount of sample is limited. Among the applications, it can be used for evaluation of disinfection through assessing the degree of denaturation for pathogens proteins.

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 Physicochemical Peculiarities of Iodine-Dimethylsulfoxide-H2O Solutions and Effect on Ion Binding to Bovine Serum Albumin

2013 ◽  
Vol 2013 ◽  
pp. 1-5
Author(s):  
K. Grigoryan ◽  
H. Shilajyan
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Electrostatic Interactions ◽  
Entropy Change ◽  
Ion Binding ◽  
Fluorescence Energy Transfer ◽  
Iodide Ion ◽  
Different Temperatures ◽  
Fluorescence Energy

The interaction of iodine with bovine serum albumin (BSA) in dimethylsulfoxide (DMSO) aqueous solutions was studied by means of fluorescence and UV/Vis absorption spectroscopy methods. Physicochemical peculiarities of these solutions were revealed. The results showed that the tri-iodide ion formed in the 1DMSO : 2H2O solution caused the fluorescence quenching of BSA. The modified Stern-Volmer quenching constant and corresponding thermodynamic parameters, the free energy change (), enthalpy change (), and entropy change (), at different temperatures (293, 298, and 303 K) were calculated, which indicated that the hydrophobic and electrostatic interactions were the predominant operating forces. The binding locality distance r between BSA and tri-iodide ion at different temperatures was determined based on Förster nonradiation fluorescence energy transfer theory.

STUDY OF THE TRANSFORMATION OF NITROSYL IRON COMPLEX WITH N-ETHYLTHIOUREA LIGANDS IN MODEL BIOLOGICAL SYSTEMS

2021 ◽  
Author(s):  
Olesya Viktorovna Pokidova ◽  
◽  
Nina Sergeevna Emel’yanova ◽  
Alexander Vasilievich Kulikov ◽  
Alexander Ivanovich Kotelnikov ◽  
...  
Keyword(s):  
Amino Acid ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Reduced Glutathione ◽  
Decay Product ◽  
Iron Complex ◽  
Amino Acid Residues ◽  
Cationic Complex ◽  
Nitrosyl Iron Complex

The process of transformation of a mononuclear cationic complex with N-ethylthiourea ligands in Tris-HCl buffer, as well as in a reaction mixture with reduced glutathione and bovine serum albumin, has been studied. It was found that in the presence of glutathione, the complex dimer-izes, while its initial ligands are replaced by glutathione. In the presence of albumin, the decay product of the complex is coordinated with amino acid residues (Cys34 and His39) to form a protein-bound complex.

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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