Effects of clustering structure on volumetric properties of amino acids in (DMSO + water) mixtures |
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| Affiliation: | 1. Guangxi Key Laboratory of Petrochemical Resource Processing and Process Intensification Technology, College of Chemistry and Chemical Engineering, Guangxi University, Nanning 530004, China;2. Department of Chemistry and Chemical Engineering, Zaozhuang University, Zaozhuang 277160, China;3. Department of Chemistry, Zhejiang University, Hangzhou 310027, China;1. Université Paris Est, Institut de Chimie et des Matériaux Paris-Est (UMR 7182), CNRS, UPEC, 2-8 rue Henri Dunant, F-94320 Thiais, France;2. Univ Lyon, Université Claude Bernard – Lyon 1, CNRS, IRCELYON – UMR 5256, 2 Avenue Albert Einstein, F-69626 Villeurbanne Cedex, France;1. Institute of Organic Chemistry, National Academy of Sciences of the Ukraine, Murmanskaya St., 5, UA-02094, Kyiv, Ukraine;2. Department of Chemistry, Taras Shevchenko National University of Kyiv, 64/13, Volodymyrska Str. Kyiv, 01601, Ukraine;3. The Chemours Company, 200 Powder Mill Rd., Experimental Station Wilmington, DE, 19803, USA;1. CanAm Bioresearch Inc., Winnipeg, MB R3T 0P4 Canada;2. Department of Chemistry, Wayne State University Detroit, Rm 185 Chemistry, MI 48202, USA;3. Phenomenex Inc., Torrance, CA 90501, USA;1. Key Laboratory of Cryogenics, Technical Institute of Physics and Chemistry, Chinese Academy of Sciences, P.O. Box 2711, Beijing 100190, China;2. University of Chinese Academy of Sciences, Beijing 100039, China |
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| Abstract: | For a better understanding on the functions of DMSO in biological systems at a relatively lower concentration, apparent molar volumes of three typical amino acids, glycine, l-alanine and l-serine in (DMSO + water) mixtures were determined and the transfer volumes from water to the mixtures were evaluated. Together with static light scattering measurement, the results were utilised to reveal the microscopic solvent structure of (DMSO + water) mixtures and its influence on the interaction between DMSO and amino acids from a clustering point of view. The results demonstrate that the interaction between amino acids and DMSO is greatly related to the clustering structure of the mixed solvent and that amino acids interacted with already established solvent clusters. The linear dependence of transfer volume of amino acids on DMSO concentration up to 2.0 mol ⋅ dm−3 could be attributed to the increasing interaction with (DMSO)1(H2O)n clusters. The formation of (DMSO)m(H2O)n cluster via hydrophobic aggregating at higher DMSO concentration led to a decrease in hydrophobic effect of DMSO and its hydrophobic–hydrophilic and hydrophobic–hydrophobic interaction with amino acids. The structure change of solvent and the interaction between amino acid residues and DMSO was reflected by the solvation of proteins. It was found that dependence of hydrodynamic radius of bovine serum albumin and lysozyme on DMSO concentration was the same and similar to that of static light scattered by the mixed solvent, regardless of the difference in conformational change between the two proteins. |
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