Role of ionic liquids in protein refolding: native/fibrillar versus treated lysozyme

TL;DR

This study investigates how ammonium-based ionic liquids, especially Ethyl Ammonium Nitrate, enhance protein refolding, demonstrating Raman spectroscopy as an effective diagnostic tool for analyzing refolding processes.

Contribution

It demonstrates the refolding enhancement capability of ammonium-based ionic liquids on lysozyme and highlights Raman spectroscopy's utility in monitoring protein refolding.

Findings

EAN is the most effective IL for lysozyme refolding

Raman spectra confirm structural recovery of lysozyme

Ionic liquids can significantly improve protein refolding processes

Abstract

Several ionic liquids (ILs) are known to revert aggregation processes and improve the in vitro refolding of denatured proteins. In this paper the capacity of a particular class of ammonium based ILs to act as refolding enhancers was tested using lysozyme as a model protein. Raman spectra of ILs treated fibrillar lysozyme as well as lysozyme in its native and fibrillar conformations were collected and carefully analyzed to characterize the refolding extent under the effect of the IL interaction. Results obtained confirm and largely extend the earlier knowledge on this class of protic ILs and indicate Ethyl Ammonium Nitrate (EAN) as the most promising additive for protein refolding. The experiment provides also the demonstration of the high potentiality of Raman spectroscopy as a comprehensive diagnostic tool in this field.