Evaluation of the toxicity of ionic liquids on trypsin: A mechanism study

The toxicity of ionic liquids (Is) was evaluated by using trypsin as biomarker. Experimental results indicated that the trypsin activity was inhibited by ILs and the degree of inhibition highly depended on the chemical structures of ILs. Primary analysis illustrated that hydrophobicity of ILs was one of the driven forces ruling the ILs-trypsin interaction. Thermodynamic parameters, Gibbs free energy change (Delta G), enthalpy change (Delta H) and entropy change (Delta S) were obtained by analyzing the fluorescence behavior of trypsin in the presence of ILs. Both negative Delta H and Delta S suggested hydrogen bonding was the major driven force underlying the IL-trypsin interaction. To assess the toxicity of ILs, it should be considered the combination of the hydrogen bonding ability and hydrophobicity of ILs. A regression based model was established to correlate the relationship of the inhibitory ability, hydrophobicity and hydrogen bonding ability of ILs. (C) 2016 Elsevier Ltd. All rights reserved.