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.

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.

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 Nanocoatings of Bovine Serum Albumin on Glass: Effects of pH and Temperature

2020 ◽  
Vol 2020 ◽  
pp. 1-11
Author(s):  
Sergio-Miguel Acuña-Nelson ◽  
José-Miguel Bastías-Montes ◽  
Fabiola-Rossana Cerda-Leal ◽  
Julio-Enrique Parra-Flores ◽  
Juan-Salvador Aguirre-García ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Self Assembly ◽  
Glass Surface ◽  
Bovine Serum ◽  
Electrostatic Interactions ◽  
Dynamic Contact ◽  
Dlvo Theory ◽  
Contact Angles ◽  
Protein Size

Protein adsorption is influenced by many factors such as temperature, pH, protein size and structure, or surface energy and roughness, among others. Self-assembled monolayers (SAMs) and the Langmuir-Blodgett (LB) technique are two of the techniques more used to produces ultrathin films of proteins on surfaces. In this work, we established protocols for the preparation of nanocoatings of bovine serum albumin (BSA) protein on glass surface using SAMs and LB. Furthermore, we determined how small changes in temperature and pH can affect the covering when SAMs are used. Using a combination of different analyses, such as relative roughness, dynamic contact angles, and atomic force microscopy (AFM), it was possible to establish conditions to obtain a uniform nanocoating using SAMs. The results of the analysis of the nanocoating performed using the LB technique were very similar to those obtained using SAMs. The Derjaguin–Landau–Verwey–Overbeek (DLVO) theory in conjunction with the AFM images showed that electrostatic interactions are very important in the self-assembly process, but a process dominated solely by attraction is not sufficient to achieve a good SAM nanocoating, since it does not allow proper orientation and packaging of BSA molecules on the glass surface.

Synthesis, crystal structure and bovine serum albumin–binding studies of a new Cd(II) complex incorporating 2,2′-(propane-1,3-diyl)bis(1H-imidazole-4,5-dicarboxylate)

2019 ◽  
Vol 44 (3-4) ◽  
pp. 198-205 ◽  
Author(s):  
Xiao-Fei Li ◽  
Li-Gang Ma ◽  
Yan-Qiu Yang ◽  
Yan-Ju Liu ◽  
Xiang-Ru Meng ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Three Dimensional ◽  
Entropy Change ◽  
Chain Structure ◽  
Binding Studies ◽  
Carboxylate Oxygen ◽  
Fluorescence Measurements ◽  
Bovine Serum Albumin Binding

A new Cd(II) complex, [Cd(H4pbidc)(H2O)] n (1), incorporating 2,2′-(propane-1,3-diyl)bis(1H- imidazole-4,5-dicarboxylic acid) (H6pbidc) was synthesized and characterized by elemental analysis, infrared spectra and X-ray single-crystal diffraction. In complex 1, each Cd(II) ion is hepta-coordinated, showing a significantly distorted pentagonal-bipyramidal coordination environment. Adjacent Cd(II) ions are alternately joined through two carboxylate oxygen atoms and two bridging water molecules resulting in a one-dimensional chain structure. In the solid state, adjacent chains are further linked by hydrogen bonds, forming a three-dimensional supramolecular architecture. Meanwhile, the interactions of complex 1 with bovine serum albumin were analysed by fluorescence measurements under physiological conditions. The results indicated that the fluorescence intensity of bovine serum albumin was decreased considerably upon the addition of complex 1 through a static quenching mechanism with formation of one binding site. The negative values of the thermodynamic parameters including enthalpy change (Δ H), entropy change (Δ S) and Gibbs free energy change (Δ G) showed that hydrogen bonding and van der Waals forces were the main interactions in the binding of complex 1 to bovine serum albumin, and the binding process is spontaneous in thermodynamics.

scholarly journals Spectroscopic Studies of the Interaction between Metformin Hydrochloride and Bovine Serum Albumin

2012 ◽  
Vol 11 (1) ◽  
pp. 45-49 ◽  
Author(s):  
Ahmad Tanwir ◽  
Rahat Jahan ◽  
Mohiuddin Abdul Quadir ◽  
Mohammad A Kaisar ◽  
Md Khalid Hossain
Keyword(s):  
Hydrogen Bond ◽  
Bovine Serum Albumin ◽  
Fluorescence Quenching ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Spectroscopic Studies ◽  
Metformin Hydrochloride ◽  
Tryptophan Residue ◽  
Different Temperatures ◽  
Hoff Equation

The affinity of a drug to serum albumin has influence on the pharmacokinetics of a drug. In the present study, the mutual interaction of metformin hydrochloride (MET) with bovine serum albumin (BSA) was investigated using fluorescence spectroscopy under different conditions. It was observed that the fluorescence  quenching of BSA by metformin hydrochloride is a result of the formation of metformin hydrochloride- BSA complex with probable involvement of tryptophan residue. Fluorescence quenching constants were determined using  the Stern- Volmer equation and Van’t Hoff equation to provide a measure of the thermodynamic parameters ?G, ?H, and ?S at different temperatures indicating that the hydrogen bond and the hydrophobic forces play a major role for metformin hydrochloride- BSA association. DOI: http://dx.doi.org/10.3329/dujps.v11i1.12486 Dhaka Univ. J. Pharm. Sci. 11(1): 45-49, 2012 (June)

Contribution of Surface Charge to Bovine Serum Albumin Adsorption on Hydroxyapatite Ceramic Particles

2007 ◽  
Vol 330-332 ◽  
pp. 861-864 ◽  
Author(s):  
Xiang Dong Zhu ◽  
Hong Song Fan ◽  
X. N. Chen ◽  
Dong Xiao Li ◽  
Xing Dong Zhang
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Surface Charge ◽  
Bovine Serum ◽  
Electrostatic Interactions ◽  
Solid Particles ◽  
Hydroxyapatite Ceramic ◽  
Liquid Environment ◽  
Zeta Potentials ◽  
Albumin Adsorption

Protein adsorption is driven by various interactions. The contribution of surface charge to bovine serum albumin (BSA) adsorption on hydroxyapatite (HA) ceramic was investigated by adjusting the liquid environment in which the solid particles dispersed. Zeta potentials of HA and the adsorption of BSA on the surface were tested as a function of pH, ionic strength, Ca2+ and PO4 3- concentrations in the aqueous solutions, and the results showed that both of them were greatly affected by those experimental variations. Besides, the amount of adsorbed BSA was related to the variation of zeta potential of HA, as could be well understood in terms of electrostatic interactions.

scholarly journals Insight into the Interaction between the HIV-1 Integrase Inhibitor Elvitegravir and Bovine Serum Albumin: A Spectroscopic Study

2015 ◽  
Vol 2015 ◽  
pp. 1-9 ◽  
Author(s):  
Ali Saber Abdelhameed
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Absorption Spectra ◽  
Bovine Serum ◽  
Average Distance ◽  
Three Dimensional ◽  
Integrase Inhibitor ◽  
Visible Absorption ◽  
Spontaneous Interaction ◽  
Different Temperatures

The interaction between the anti-HIV drug Elvitegravir (EVG) and bovine serum albumin (BSA) was investigated by fluorescence spectroscopy and UV-visible absorption spectra. The mechanism for quenching the fluorescence of BSA by EVG is discussed. It was found that EVG can quench the intrinsic fluorescence of BSA through a static quenching procedure. The quenching type, association constant, and number of binding sites were investigated. The binding constant of EVG with BSA was calculated at different temperatures based on fluorescence quenching results. The thermodynamic parametersΔHθ,ΔGθ, andΔSθwere determined. The positiveΔSθand negativeΔHθandΔGθvalues showed that a spontaneous interaction may involve both roles of hydrophobic interaction and hydrogen bonding. The interaction of BSA with EVG was also confirmed by UV absorption spectra. The average distance,r, between donor (BSA) and acceptor (EVG) was obtained according to Förster’s theory of nonradiation energy transfer. Synchronous fluorescence and three-dimensional fluorescence spectra were used to investigate the conformational change of BSA molecules that occur upon addition of EVG and showed, upon binding, a possibility of increasing hydrophobicity around tryptophan residues of BSA.

scholarly journals Spectral study of coumarin-3-carboxylic acid interaction with human and bovine serum albumins

2011 ◽  
Vol 9 (4) ◽  
pp. 624-634 ◽  
Author(s):  
Aurica Varlan ◽  
Mihaela Hillebrand
Keyword(s):  
Carboxylic Acid ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Electrostatic Interactions ◽  
Resonance Energy ◽  
Entropy Change ◽  
Cd Spectroscopy ◽  
Binding Studies ◽  
Serum Albumins ◽  
Buffer Solution

AbstractFluorescence spectroscopy and circular dichroism (CD) spectroscopy were used to investigate the interaction of coumarin-3-carboxylic acid with human serum albumin (HSA) and bovine serum albumin (BSA) under physiological conditions in a buffer solution of pH 7.4. Quenching constants were determined using the Lineweaver-Burk equation to provide a measure of the binding affinity of coumarin-3-carboxylic acid to HSA/BSA. Binding studies concerning the number of binding sites, n, and apparent binding constant, K, were performed by a fluorescence quenching method at different temperatures (298, 303 and 310 K). The thermodynamic parameters, enthalpy change (ΔH0) and entropy change (ΔS0) as calculated according to the van’t Hoff equation, indicated that hydrogen bonding and van der Waals forces play a major role in coumarin-3-carboxylic acid-HSA association whereas electrostatic interactions dominate in coumarin-3-carboxylic acid-BSA association. The distance, r, between the donor (HSA/BSA) and acceptor (coumarin-3-carboxylic acid) has been estimated using Förster’s equation, on the basis of resonance energy transfer. Furthermore, CD spectra were used to investigate the α-helix changes of the HSA and BSA molecules upon addition of coumarin-3-carboxylic acid.

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