Abstract
In this work, N-1 substituted 1,2,4-triazolium-based cation and trifluoromethanesulfonate anion based IL has been synthesized and used as a solvent system to stabilize haemoglobin (Hb). The conformational stability of Hb at different concentrations of developed IL was inspected through spectroscopic techniques like UV–Vis, steady-state fluorescence, fluorescence time-correlated single photon counting (TCSPC), temperature dependent UV–Vis, fluorescence, and circular dichroism (CD). Hb structure is stabilized in the IL concentration range 0.001 to 0.01 M; Hb structure starts opening up in the IL concentration range 0.05 to 0.1 M; at 0.2 M IL concentration, denaturation of Hb takes place. Further, the nature of the interaction between IL and Hb was verified through a competitive hydrophobic fluorescence probe, 1-Anilino-8-Naphthalene Sulfonate (ANS), and it was observed that ANS does not interact with IL till 0.01 M IL concentration. Finally, the experiments illustrate that the IL concentration plays a significant role in stabilizing/destabilizing a particular protein.
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