Adsorption and Conformation of Bovine Serum Albumin on Montmorillonite: Modification of the Balance between Hydrophobic and Electrostatic Interactions by Protein Methylation and pH Variation

1994 ◽  
Vol 166 (1) ◽  
pp. 89-94 ◽  
Author(s):  
S. Staunton ◽  
H. Quiquampoix
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Electrostatic Interactions ◽  
Protein Methylation ◽  
Ph Variation

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 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.

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 Complex coacervates between bovine serum albumin and anionic polysaccharides: formation and characterization

2021 ◽  
Vol 24 ◽  
Author(s):  
Lorena Oliveira Ferreira ◽  
Monique Barreto Santos ◽  
Edwin Elard Garcia-Rojas
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Electrostatic Interactions ◽  
Initial Study ◽  
Wide Ph Range ◽  
The Fourier Transform ◽  
Ph Range ◽  
The Comparative Study ◽  
Maximum Turbidity

Abstract The comparative study regarding complexes coacervated between Bovine Serum Albumin (BSA) and different polysaccharides, Pectin (PEC) and Gum Acacia (GA), was carried out by evaluating the influence of different ratios (protein:polysaccharide) and sodium chloride (NaCl) concentrations on turbidity and zeta potential. The BSA:PEC complexes were formed in a 10:1 ratio whereas BSA:GA at 3:1. The complexation pH showed different behavior, BSA: PEC complexes exhibited maximum turbidity in a wide pH range (4.9 to 1.5), while BSA: GA had maximum turbidity at pH 3.5. The increase in the concentration of NaCl negatively influenced the complexation. The NaCl concentration of 0.40 mol L-1 suppressed the interaction in BSA:PEC (10:1) and reduced the range formation of BSA:GA (3:1). The Fourier Transform Infrared (FTIR) demonstrated the participation not only of electrostatic interactions, but also of hydrogen bonds in the complexation. This initial study elucidated fundamental aspects about the formation of coacervate complexes between BSA:GA/PEC that assist in directing its application in food products especially, in acidic matrices (pH~4.0) as well as with low concentration of salts, in view of the effect of pH on maximum formation and sensitivity to NaCl. These complexes can be added directly to products in order to add nutritional value or even be used as a new matrix for the encapsulation of bioactive compounds.

scholarly journals Fluorescence Spectroscopy Study on the Interaction between Evodiamine and Bovine Serum Albumin

2013 ◽  
Vol 2013 ◽  
pp. 1-6 ◽  
Author(s):  
Mingxiong Tan ◽  
Weijiang Liang ◽  
Xujian Luo ◽  
Yunqiong Gu
Keyword(s):  
Bovine Serum Albumin ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Electrostatic Interactions ◽  
Association Constants ◽  
Experimental Results ◽  
Spectroscopy Study ◽  
Serum Albumins ◽  
Two Temperatures

The interaction of evodiamine (Evo) with bovine serum albumins (BSAs) at different two temperatures (298 and 310 K) was investigated by means of fluorescence spectroscopy. The experimental results showed that Evo binds with BSA via a static quenching procedure with association constantsKof1.61×106 L/mol at 298 K and6.78×105 L/mol at 310 K. The number of bound Evo molecules per protein is 1.31 at 298 K and 1.33 at 310 K. The results suggested that Evo reacts with BSA chiefly through hydrophobic and electrostatic interactions, and it does not alter theα-helical nature of BAS.

scholarly journals Molecular Modeling and Spectroscopic Studies on the Interaction of Transresveratrol with Bovine Serum Albumin

2013 ◽  
Vol 2013 ◽  
pp. 1-7 ◽  
Author(s):  
Xiaoli Liu ◽  
Yonghui Shang ◽  
Xudong Ren ◽  
Hua Li
Keyword(s):  
Molecular Modeling ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Conformational Changes ◽  
Binding Sites ◽  
Bovine Serum ◽  
Electrostatic Interactions ◽  
Binding Constants ◽  
Binding Mode ◽  
Spectroscopic Studies

The interaction of transresveratrol (TRES) with bovine serum albumin (BSA) has been investigated by ultraviolet-visible, fluorescence, Fourier transform infrared spectroscopic methods and molecular modeling techniques. The fluorescence results show that the intrinsic fluorescence of BSA is quenched by TRES through a static quenching procedure. The binding constants of TRES with BSA at 292, 297 and 302 K are calculated as10.22×104,8.71×104, and7.59×104 L mol−1, respectively, and corresponding numbers of binding sites are approximately equal to unity. The thermodynamic parameters ΔHand ΔSare estimated to be −21.82 kJ mol−1and +21.15 J mol−1 K−1, which indicates that the interaction of TRES with BSA is driven mainly by hydrophobic forces and there are also hydrogen bonds and electrostatic interactions. The competitive experiments suggest that the binding site of TRES to BSA is probably located on site II. The results of infrared spectra show that the binding of TRES with BSA leads to conformational changes of BSA, and the binding stabilizes theα-helix andβ-sheet at the cost of a corresponding loss in theβ-turn structure of BSA. The results of molecular modeling calculation clarify the binding mode and the binding sites which are in good accordance with the experiment results.

Influence of DNA, Alginate, Lysozyme and Bovine Serum Albumin on Sodium Silicate Condensation

2002 ◽  
Vol 724 ◽  
Author(s):  
Thibaud Coradin ◽  
Aurélie Coupé ◽  
Jacques Livage
Keyword(s):  
Bovine Serum Albumin ◽  
Hydrogen Bonds ◽  
Serum Albumin ◽  
Sodium Silicate ◽  
Bovine Serum ◽  
Electrostatic Interactions ◽  
Weak Interactions ◽  
Silica Gels ◽  
Peptide Chain ◽  
Organic Species

AbstractThe interaction of DNA, alginate, Lysozyme and Bovine Serum Albumin with diluted solutions of sodium silicate was studied using the molybdosilicate method. DNA and alginate showed very weak interactions with silica precursors whereas both proteins were able to form silica gels. Both electrostatic interactions and hydrogen bonds are suggested to arise between peptide chain and polysilicates, bringing new informations on the nature of inorganic and bio-organic species involved in the natural biosilicification processes.

scholarly journals Polycomplexes of Bovine Serum Albumin with Poly[2-Methacryloyloxy) Ethyl]Trimethyl Ammonium Chloride

2017 ◽  
Vol 4 (3) ◽  
pp. 195 ◽  
Author(s):  
Vitaliy V. Khutoryanskiy ◽  
Zauresh S. Nurkeeva ◽  
Grigoriy A. Mun ◽  
Natalie L. Rebenchuk ◽  
Anatoliy T. Ivaschenko ◽  
...  
Keyword(s):  
Ionic Strength ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Ammonium Chloride ◽  
Bovine Serum ◽  
Electrostatic Interactions ◽  
Ph Value ◽  
Solution Concentration ◽  
Water Soluble ◽  
Trimethyl Ammonium Chloride

Complex formation between bovine serum albumin and water-soluble synthetic cationic polyelectrolyte poly[2-methacryloyloxy)ethyl]trimethyl ammonium chloride has been studied in aqueous solutions by turbidimetric and viscometric methods. It was found that the structure of polycomplex is compact and its stability strongly depends on the environment. Formation of insoluble polycomplexes is observed in solutions with low ionic strength and pH, higher than 5.0. This pH value corresponds to the isoelectric point of the protein, so at lower pH the biopolymer macromolecules gain the positive charge and not able to be bound by the positively charged macromolecules of poly[2-methacryloyloxy)ethyl]trimethyl ammonium chloride. An increase of pH within 5.0-11.0 leads to further stabilization of polycomplex because of appearance of additional negative charges on biomacromolecules, caused by ionization of acidic groups. It was found that the main forces, which are responsible for the complexation, are electrostatic interactions.<br />The intensity of the complexation is dependent on the solution concentration, pH and ionic strength. In solutions with high ionic strength (I=0.2, 1.0) the mixing of the reagents does not lead to the formation of insoluble polycomplexes. The observed dependence is connected with the screening of electrostatic interactions between macromolecules of the biopolymer and synthetic polyelectrolyte by small ions present in solution.

scholarly journals In silico and multi-spectroscopic analyses on the interaction of 5-amino-8-hydroxyquinoline and bovine serum albumin as a potential anticancer agent

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Waralee Ruankham ◽  
Kamonrat Phopin ◽  
Ratchanok Pingaew ◽  
Supaluk Prachayasittikul ◽  
Virapong Prachayasittikul ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Serum Protein ◽  
In Silico ◽  
Bovine Serum ◽  
Electrostatic Interactions ◽  
Water Solubility ◽  
Free Fraction ◽  
Amino Derivative

Abstract5-Amino-8-hydroxyquinoline (5A8HQ), an amino derivative of 8-hydroxyquinoline, has become a potential anticancer candidate because of its promising proteasome inhibitory activity to overcome and yet synergize bortezomib for fighting cancers. Therefore, in this study, its physicochemical properties and interaction activities with serum protein have extensively been elucidated by both in vitro and in silico approaches to fulfill the pharmacokinetic and pharmacodynamic gaps. 5A8HQ exhibited the drug-likeness properties, where oral administration seems to be a route of choice owing to its high-water solubility and intestinal absorptivity. Multi-spectroscopic investigations suggested that 5A8HQ tended to associate with bovine serum albumin (BSA), a representative of serum protein, via the ground-state complexation. It apparently bound in a protein cleft between subdomains IIA and IIIA of BSA as suggested by the molecular docking and molecular dynamics simulations. The binding was mainly driven by hydrogen bonding and electrostatic interactions with a moderate binding constant at 104 M−1, conforming with the predicted free fraction in serum at 0.484. Therefore, 5A8HQ seems to display a good bioavailability in plasma to reach target sites and exerts its potent pharmacological activity. Likewise, serum albumin is a good candidate to be reservoir and transporter of 5A8HQ in the circulatory system.

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