Mechanism of Phosphate Adsorption to a Three-Dimensional Structure of Boehmite in the Presence of Bovine Serum Albumin

1993 ◽  
Vol 82 (7) ◽  
pp. 744-749 ◽  
Author(s):  
Akira Ookubo ◽  
Mikio Nishida ◽  
Kenta Ooi ◽  
Keisuke Ishida ◽  
Yuko Hashimura ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Phosphate Adsorption ◽  
Three Dimensional Structure

scholarly journals Three-dimensional structure of human serum albumin

Science ◽  
1989 ◽  
Vol 244 (4909) ◽  
pp. 1195-1198 ◽  
Author(s):  
D. Carter ◽  
X. He ◽  
S. Munson ◽  
P. Twigg ◽  
K. Gernert ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Three Dimensional Structure

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.

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 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 Interaction of Conazole Pesticides Epoxiconazole and Prothioconazole with Human and Bovine Serum Albumin Studied Using Spectroscopic Methods and Molecular Modeling

2021 ◽  
Vol 22 (4) ◽  
pp. 1925
Author(s):  
Katarína Golianová ◽  
Samuel Havadej ◽  
Valéria Verebová ◽  
Jozef Uličný ◽  
Beáta Holečková ◽  
...  
Keyword(s):  
Molecular Modeling ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Three Dimensional ◽  
Association Constants ◽  
Van Der Waals Interactions ◽  
Spectroscopic Methods ◽  
Spectroscopic Techniques ◽  
Conformation Changes

The interactions of epoxiconazole and prothioconazole with human serum albumin and bovine serum albumin were investigated using spectroscopic methods complemented with molecular modeling. Spectroscopic techniques showed the formation of pesticide/serum albumin complexes with the static type as the dominant mechanism. The association constants ranged from 3.80 × 104–6.45 × 105 L/mol depending on the pesticide molecule (epoxiconazole, prothioconazole) and albumin type (human or bovine serum albumin). The calculated thermodynamic parameters revealed that the binding of pesticides into serum albumin macromolecules mainly depended on hydrogen bonds and van der Waals interactions. Synchronous fluorescence spectroscopy and the competitive experiments method showed that pesticides bind to subdomain IIA, near tryptophan; in the case of bovine serum albumin also on the macromolecule surface. Concerning prothioconazole, we observed the existence of an additional binding site at the junction of domains I and III of serum albumin macromolecules. These observations were corroborated well by molecular modeling predictions. The conformation changes in secondary structure were characterized by circular dichroism, three-dimensional fluorescence, and UV/VIS absorption methods.

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