Evaluation of the toxicity of ionic liquids on trypsin: A mechanism study.
Chemosphere
; 148: 241-7, 2016 Apr.
Article
en En
| MEDLINE
| ID: mdl-26807945
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.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Tripsina
/
Contaminantes Ambientales
/
Líquidos Iónicos
Límite:
Animals
Idioma:
En
Revista:
Chemosphere
Año:
2016
Tipo del documento:
Article
País de afiliación:
China