Dataset Information

Influence of pH and Salts on Partial Molar Volume of Lysozyme and Bovine Serum Albumin in Aqueous Solutions.

ABSTRACT: The partial molar volume of lysozyme and bovine serum albumin in aqueous solutions at different pH values and in aqueous solutions containing sodium chloride, ammonium chloride, sodium sulfate, or ammonium sulfate at different concentrations at pH?7.0 was investigated experimentally at 298.15?K and 1?bar. It was found that the influence of the pH value and the salts on the partial molar volume of the proteins is small, but trends were measurable. Furthermore, the partial molar volume of lysozyme in pure water at different pH values and in aqueous solutions with different sodium chloride concentrations at pH?7.0 was predicted by molecular simulations. The predictions are in good agreement with the experimental data.

SUBMITTER: Jirasek F

PROVIDER: S-EPMC6472598 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature

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Influence of pH and Salts on Partial Molar Volume of Lysozyme and Bovine Serum Albumin in Aqueous Solutions.

Jirasek Fabian F Garcia Edder J EJ Hackemann Eva E Galeotti Nadia N Hasse Hans H

Chemical engineering & technology 20181023 12

The partial molar volume of lysozyme and bovine serum albumin in aqueous solutions at different pH values and in aqueous solutions containing sodium chloride, ammonium chloride, sodium sulfate, or ammonium sulfate at different concentrations at pH 7.0 was investigated experimentally at 298.15 K and 1 bar. It was found that the influence of the pH value and the salts on the partial molar volume of the proteins is small, but trends were measurable. Furthermore, the partial molar volume of lysozyme ...[more]

PMID: 31007400

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Project description:Herein, we have investigated the interaction of bovine serum albumin (BSA), the most abundant globular protein, with a conventional cationic surfactant, cetyldimethylethylammonium bromide (CDMEAB), through a conductivity technique in the absence/presence of electrolyte solutions at various temperatures (298.15-323.15 K). The interaction of the protein with drugs/surfactants and other additives plays a crucial role in the body. Hence, the main concern of the study is to extract the impact of BSA on surfactant molecules and vice versa. From the specific conductivity versus concentration of surfactant plots, three different noticeable critical micelle concentration (c*) values were obtained for pure CDMEAB and its mixture with protein/protein + salts. The presence of BSA and electrolytes altered the c* values of CDMEAB revealing interactions among the studied constituents where the salt solutions reduced the c* values and created a convenient environment for favorable micellization. The negative magnitudes achieved for standard free energy changes (ΔG 0 m) suggest spontaneity of micellization while the values of ΔH 0 m and ΔS 0 m signified the existence of some electrostatic and hydrophobic interactions. The values of molar heat capacity (ΔC 0 m) were positive as well as small which was an indication of less structural deformation. Molecular Dynamics (MD) simulation for all atoms revealed that the salt ions promoted non-covalent interaction between BSA and CDMEAB, and such interactions were not observed in the absence of the salt. Protein structure remained nearly same in spite of strong interaction with CDMEAB as evident from the overall RMSD (root-mean-square deviation) values of the alpha carbons and backbone of the protein and RMSF (root-mean-square fluctuation) values of the amino acid residues present in BSA. In this work thermodynamic parameters of transfer (such as ΔG 0 m.tr., ΔH 0 m.tr., and ΔC 0 p.m.tr.) were also evaluated and the results are discussed in detail. Besides, contributions of enthalpy and entropy to free energy changes were also analyzed.

Dataset Information

Influence of pH and Salts on Partial Molar Volume of Lysozyme and Bovine Serum Albumin in Aqueous Solutions.

Publications

Influence of pH and Salts on Partial Molar Volume of Lysozyme and Bovine Serum Albumin in Aqueous Solutions.

Similar Datasets

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