Thermodynamic contributions of peptide backbone unit from water to biocompatible ionic liquids at T = 298.15 K

T. Vasantha, Pankaj Attri, Pannuru Venkatesu, R. S. Rama Devi

研究成果: ジャーナルへの寄稿学術誌査読

31 被引用数 (Scopus)


To quantify the biomolecular interactions of protein functional groups with biocompatible ionic liquids (ILs), transfer free energies (ΔGtr′) of model compounds from water to aqueous ILs solutions have been determined from the solubility measurements, as a function of ILs concentration at T = 298.15 K under atmospheric pressure. The aqueous systems investigated contain amino acids of zwitterionic glycine peptides: glycine (Gly), diglycine (Gly 2), and cyclic glycylglycine (c(GG)) with ILs of diethylammonium acetate ([Et2NH][CH3COO], DEAA), triethylammonium acetate ([Et3NH][CH3COO], TEAA), and trimethylammonium acetate ([Me3NH][CH3COO], TMAA). It was found that the solubility of model compounds in aqueous IL solutions decreases with increasing IL concentration (salting-out effect). We observed positive values of ΔGtr′ for Gly, Gly2, and c(GG) from water to ILs, indicating that the interactions between ILs and protein surface are unfavourable, which leads to stabilization of the native structure of amino acids. Moreover, our experimental data is used to determine transfer free energies (Δgtr′) of the peptide backbone unit (-CH2CONH-) from water to IL solutions. These results explicitly elucidate that all alkyl ammonium ILs acted as stabilizers for tested model compounds through the exclusion of ILs from surface of model compounds and also reflect the effect of alkyl chain on the stability of protein model compounds. To obtain the mechanism events of the ILs role in enhancing the stability of the model compounds structure, we further studied the UV-vis spectrum analysis.

ジャーナルJournal of Chemical Thermodynamics
出版ステータス出版済み - 2月 2012

!!!All Science Journal Classification (ASJC) codes

  • 原子分子物理学および光学
  • 材料科学(全般)
  • 物理化学および理論化学


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