Effects of Ionic Liquid Alkyl Chain Length on Denaturation of Myoglobin by Anionic, Cationic, and Zwitterionic Detergents.

摘要: The unique electrochemical properties of ionic liquids (ILs) have motivated their use as solvents for organic synthesis and green energy applications. More recently, potential in pharmaceutical chemistry has prompted investigation into effects on biomolecules. There is evidence that some ILs can destabilize proteins via a detergent-like manner; however, the mechanism still remains unknown. Our hypothesis if are denaturing mechanism, detergent-mediated protein unfolding should be enhanced presence ILs. myoglobin was examined zwitterionic (N,N-dimethyl-N-dodecylglycine betaine (Empigen BB®, EBB)), cationic (tetradecyltrimethylammonium bromide (TTAB)), anionic (sodium dodecyl sulfate (SDS)) detergent well based alkylated imidazolium chlorides. Protein structure measured through combination absorbance, fluorescence, circular dichroism (CD) spectroscopy: absorbance CD were used to monitor heme complexation myoglobin, tryptophan fluorescence quenching an indicator dissociation. Notably, detergents tested did not fully denature but instead resulted loss group. At low IL concentrations, dissociation remained traditional, cooperative process; at high with increased character exhibited more complex pattern, which most likely attributable micellization or direct denaturation induced by These trends consistent across all species detergents. 1,6-diphenyl-1,3,5-hexatriene (DPH) further characterize micelle formation aqueous solutions containing liquid. thermodynamics show EBB- TTAB-induced significantly impacted room temperature (RTILs), whereas SDS-induced dramatically RTILs examined. Together, these results indicate interaction detergents, headgroup charge, active component influence potentially denaturation.