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 Molecular imprinting of bovine serum albumin and lysozyme within the matrix of polyampholyte hydrogels based on acrylamide, sodium salt of 2-acrylamido-2-methyl-1-propanesulfonic acid and (3-acrylamidopropyl)trimethyl ammonium chloride

2021 ◽  
pp. 4-11
Author(s):  
Alexey Shakhvorostov ◽  
Sarkyt Kudaibergenov
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Ammonium Chloride ◽  
Sodium Salt ◽  
Bovine Serum ◽  
In Situ Polymerization ◽  
Trimethyl Ammonium Chloride ◽  
Cationic Monomer ◽  
The Matrix ◽  
Adsorption Desorption

Molecularly-imprinted polyampholyte (MIP) hydrogels based on nonionic monomer – acrylamide (AAm), anionic monomer – sodium salt of 2-acrylamido-2-methyl-1-propanesulfonic acid (AMPS) and cationic monomer – (3-acrylamidopropyl)trimethyl ammonium chloride (APTAC) were obtained by immobilization of bovine serum albumin (BSA) and lysozyme in situ polymerization conditions. It was found that the best amphoteric hydrogel for sorption of BSA is APTAC-75H while for sorption of lysozyme is AMPS-75H. The sorption capacity of APTAC-75H and AMPS-75H with respect to BSA and lysozyme is 305.7 and 64.1-74.8 mg per 1 g of hydrogel respectively. Desorption of BSA and lysozyme from MIP template performed by aqueous solution of 1M NaCl is equal to 82-88%. Separation of BSA and lysozyme from their mixture was performed on MIP templates. The results of adsorption-desorption cycles of BSA on adjusted to BSA polyampholyte hydrogel APTAC-75H and of lysozyme on adjusted to lysozyme polyampholyte hydrogel AMPS-75H show that the mixture of BSA and lysozyme can be selectively separated with the help of MIP hydrogels.

Preparation and Application as Biosensor of Water-Soluble Conjugated Polyelectrolyte

2013 ◽  
Vol 538 ◽  
pp. 301-304
Author(s):  
Yi Ping Zhong ◽  
Rui Bin Hong ◽  
Bin Bin Yin ◽  
Ping Liu ◽  
Wen Ji Deng
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Water Soluble ◽  
Conjugated Polyelectrolyte ◽  
Sodium Sulfonate ◽  
Vis Spectroscopy

The water-soluble conjugated polyelectrolyte, poly[3-(1′-propyloxy-3′-sodium sulfonate) thiophene] (PTH-n3-SO3Na), was prepared. The interaction between the PTH-n3-SO3Na and bovine serum albumin (BSA) was investigated using UV-vis spectroscopy. It was found that the PTH-n3-SO3Na could be used as biosensor to detect BSA.

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.

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