Protein stability in ionic solution depends on the delicate balance between protein-ion and ion-ion interactions. To address the ion specific effects on the protein, we have examined the stability of myoglobin (Mb) in the presence of buffer and ammonium-based ionic liquids (ILs) (50%, v/v). Here, fluorescence and circular dichroism (CD) spectroscopy experiments are used to study the influence of ILs on structure and stability of Mb. Our experimental results reveal that more viscous ILs (sulphate or phosphate ions) are stabilizers and therefore more biocompatible for Mb structure. Surprisingly, the less viscous ILs such as acetate anion based ILs are destabilizers for the native structure of Mb. Our results explicitly elucidate that anion variation has significant influence on Mb stability efficiency than cation variation. This study provides insight into anion effects on protein stability and explains that the intrasolvent interactions can be leveraged to enhance the stability.
|Number of pages||10|
|Journal||International Journal of Biological Macromolecules|
|Publication status||Published - Aug 2014|
All Science Journal Classification (ASJC) codes
- Structural Biology
- Molecular Biology
- Economics and Econometrics