title: Evaluation of the toxicity of ionic liquids on trypsin: A mechanism study.
abstract: The toxicity of ionic liquids (ILs) 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 (ΔG), enthalpy change (ΔH) and entropy change (ΔS) were obtained by analyzing the fluorescence behavior of trypsin in the presence of ILs. Both negative ΔH and ΔS 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.
authors.affiliation: College of Physics and Chemistry, Henan Polytechnic University, Jiaozuo 454003, China.
authors.forename: Yunchang
authors.initials: Y
authors.lastname: Fan
authors.affiliation: College of Physics and Chemistry, Henan Polytechnic University, Jiaozuo 454003, China.
authors.forename: Xing
authors.initials: X
authors.lastname: Dong
authors.affiliation: College of Physics and Chemistry, Henan Polytechnic University, Jiaozuo 454003, China. Electronic address: linglingyan811@163.com.
authors.forename: Lingling
authors.initials: L
authors.lastname: Yan
authors.affiliation: College of Physics and Chemistry, Henan Polytechnic University, Jiaozuo 454003, China.
authors.forename: Dandan
authors.initials: D
authors.lastname: Li
authors.affiliation: College of Physics and Chemistry, Henan Polytechnic University, Jiaozuo 454003, China.
authors.forename: Shaofeng
authors.initials: S
authors.lastname: Hua
authors.affiliation: College of Physics and Chemistry, Henan Polytechnic University, Jiaozuo 454003, China.
authors.forename: Chaobing
authors.initials: C
authors.lastname: Hu
authors.affiliation: College of Physics and Chemistry, Henan Polytechnic University, Jiaozuo 454003, China.
authors.forename: Chengcheng
authors.initials: C
authors.lastname: Pan
mesh_terms: D000818:Animals; D001586:Benzoylarginine Nitroanilide / Q000737:chemistry; D001665:Binding Sites; D002417:Cattle; D004785:Environmental Pollutants / Q000737:chemistry / Q000633:toxicity*; D004795:Enzyme Stability; D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D052578:Ionic Liquids / Q000737:chemistry / Q000633:toxicity*; D008962:Models, Theoretical; D010179:Pancreas / Q000201:enzymology; D013050:Spectrometry, Fluorescence; D013379:Substrate Specificity; D013816:Thermodynamics; D014357:Trypsin / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism
chemical_list: D004785:Environmental Pollutants; D052578:Ionic Liquids; D001586:Benzoylarginine Nitroanilide; D014357:Trypsin
keywords: Fluorescence spectroscopy; Hydrogen bonding; Hydrophobicity; Ionic liquids (ILs); Trypsin