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.

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 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.

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.

New Photoactivators for Multiphoton Excited Three-dimensional Submicron Cross-linking of Proteins: Bovine Serum Albumin and Type 1 Collagen¶†

2007 ◽  
Vol 76 (2) ◽  
pp. 135-144
Author(s):  
Jonathan D. Pitts ◽  
Amy R. Howell ◽  
Rosa Taboada ◽  
Ipsita Banerjee ◽  
Jun Wang ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Three Dimensional ◽  
Cross Linking

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)

Sign in / Sign up

Export Citation Format

Share Document