Structural Basis for the Enhanced Stability of Protein Model Compounds and Peptide Backbone Unit in Ammonium Ionic Liquids
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- 作者：T. Vasantha ; Pankaj Attri ; Pannuru Venkatesu ; R. S. Rama Devi
- 刊名：The Journal of Physical Chemistry B
- 出版年：2012
- 出版时间：October 4, 2012
- 年：2012
- 卷：116
- 期：39
- 页码：11968-11978
- 全文大小：634K
- 年卷期：v.116,no.39(October 4, 2012)
- ISSN：1520-5207
文摘
Protein folding/unfolding is a fascinating study in the presence of cosolvents, which protect/disrupt the native structure of protein, respectively. The structure and stability of proteins and their functional groups may be modulated by the addition of cosolvents. Ionic liquids (ILs) are finding a vast array of applications as novel cosolvents for a wide variety of biochemical processes that include protein folding. Here, the systematic and quantitative apparent transfer free energies (螖G鈥?sub>tr) of protein model compounds from water to ILs through solubility measurements as a function of IL concentration at 25 掳C have been exploited to quantify and interpret biomolecular interactions between model compounds of glycine peptides (GPs) with ammonium based ILs. The investigated aqueous systems consist of zwitterionic glycine peptides: glycine (Gly), diglycine (Gly2), triglycine (Gly3), tetraglycine (Gly4), and cyclic glycylglycine (c(GG)) in the presence of six ILs such as diethylammonium acetate (DEAA), diethylammonium hydrogen sulfate (DEAS), triethylammonium acetate (TEAA), triethylammonium hydrogen sulfate (TEAS), triethylammonium dihydrogen phosphate (TEAP), and trimethylammonium acetate (TMAA). We have observed positive values of 螖G鈥?sub>tr for GPs from water to ILs, indicating that interactions between ILs and GPs are unfavorable, which leads to stabilization of the structure of model protein compounds. Moreover, our experimental data 螖G鈥?sub>tr is used to obtain transfer free energies (螖g鈥?/i>tr) of the peptide backbone unit (or glycyl unit) (鈥擟H2C鈺怬NH鈥?, which is the most numerous group in globular proteins, from water to IL solutions. To obtain the mechanism events of the ILs' role in enhancing the stability of the model compounds, we have further obtained m-values for GPs from solubility limits. These results explicitly elucidate that all alkyl ammonium ILs act as stabilizers for model compounds through the exclusion of ILs from model compounds of proteins and also reflect the effect of alkyl chain on the stability of protein model compounds.