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    Destabilization effect of imidazolium cation-Hofmeister anion salts on cytochrome c

    Year: 2020

    Journal: Int. J. Biol. Macromol., Volume 164, DEC 1, page 3808–3813

    Authors: Garajova, Katarina; Sedlakova, Dagmar; Berta, Martin; Gazova, Zuzana; Sedlak, Erik

    Organizations: Slovak Research and Development AgencySlovak Research and Development Agency [APVV-15-0069, APVV-18-0284]; grant agency of the Ministry of Education, Science, Research and Sport of the Slovak Republic [VEGA 2/0145/17, 2/0009/17]

    Keywords: Protein stability; Ionic liquids; Hofmeister effect; Surface tension

    We have analyzed an effect of imidazolium cation-Hofmeister anion salts on stability of basic horse heart cytochrome c (cyt c) at pH 4.5 (net charge +17). The effect of salts consisting of imidazolium cations, 1-ethyl-3-methylimidazolium (EMIm(+)) and 1-butyl-3-methylimidazolium (BMIm(+)), and five anions: chloride, bromide, iodide, nitrate, and thiocyanate on thermal and pH stability of cyt c was compared with the effect of corresponding sodium salts. Correlation between parameter of dT(trs)/d [ion] (T-trs; thermal midpoints) with surface tension changes of solvent in the presence of both imidazolium and sodium salts implies direct interaction between ions and proteins. Surprisingly, the imidazoliumsalts have more pronounced destabilization effect on highly positively charged cyt c than the corresponding sodium counterparts. Our analysis suggests the direct interaction of imidazolium cations with polypeptide chain, in analogy to guanidium cation, but the destabilization effect is significantly strengthened by decreased surface tension of imidazolium salt solvents. Comparison of an effect of imidazolium and sodium salts on acidic and alkaline transitions and to thermal transition of cyt c implies a role of hydrophobic interaction between imidazolium cation and polypeptide chain. (C) 2020 Elsevier B.V. All rights reserved.
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