Protein stability
has been a concern for researchers for a long
time as they are sensitive toward their environment. Mostly proteins
during experiments require medium that keep them stable at room temperature
(RT). Recent research utilizing ionic liquids (ILs) to stabilize protein
has gained much importance. Although a few ILs have been claimed to
suit this requirement, reported studies employ IL concentrations that
might produce irreversible denaturation and aggregation. This study
demonstrates the first report for long-term stabilization of horse
heart cytochrome c (h-cyt c) by
long-chain imidazolium ILs at far low concentration (1 mM) of IL when
stored at RT. Long-chain imidazolium ILs until now were less familiar
for their stabilizing nature toward protein. A significant increase
in the helical content of h-cyt c (dissolved state)
was observed with prolonged structural stability (secondary and tertiary)
for about 6 months in aqueous solutions of 1-methyl-3-octyl imidazolium
chloride [C8mim][Cl] and 1-decyl-3-methylimidazolium chloride
[C10mim][Cl]. The in-depth mechanism discussed suggests
interaction of ILs with amino acid residues of h-cyt c, which rigidifies the loop regions with reduced mobility; hence,
prolonged stability is achieved. The study firmly advocates the use
of long-chain imidazolium ILs as the potent inhibitor against denaturation
during storage of h-cyt c at RT.
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