The protein stability in aqueous solutions is of prime importance in various biological fields, especially in the pharmaceutical field for the development of therapeutic protein products. The stability of a protein is dependent on temperature, pressure, and most importantly on the solvent properties. Co-solvents play an important role in bringing stability towards the protein molecule. For example, Sugars and polyhydric alcohols are recognized as strong stabilizers for proteins. Recently, many research groups reported ionic liquids (ILs) as the new class of biocompatible solvents for biomolecules.
ILs not only provide a novel reaction medium but also serve as effective participants in various biological reaction processes. In view of the growing importance of ILs, our group interested to investigate the effect of ILs on protein properties such as stability, activity, and structure detainment during the refolding processes. At present, we are working on different ILs based on imidazolium, ammonium and morpholinium groups.
Reference:
L. Satish, S. Millan, and H. Sahoo*, Spectroscopic Insight into the Interaction of Bovine Serum Albumin with Imidazolium-Based Ionic Liquids in Aqueous Solution, Luminescence, 2016, Accepted.