We introduce aqueous
ionic liquid (IL) mixtures, specifically mixtures
of 1-butyl-3-imidazoliumtetrafluoroborate (BMImBF4), with
water as a minimal model of lipid bilayer membranes. Imidazolium-based
ILs are known to form clustered nanoscale structures in which local
inhomogeneities, micellar or lamellar structures, are formed to shield
hydrophobic parts of the cation from the polar cosolvent (water).
To investigate these nanostructures, dynamic light scattering (DLS)
on samples with different mixing ratios of water and BMImBF4 was performed. At mixing ratios of 50% and 45% (v/v), small and
homogeneous nanostructures can indeed be detected. To test whether,
in particular, these stable nanostructures in aqueous mixtures may
mimic the effects of phospholipid bilayer membranes, we further investigated
their interaction with myelin basic protein (MBP), a peripheral, intrinsically
disordered membrane protein of the myelin sheath. Using dynamic light
scattering (DLS), continuous wave (CW) and pulse electron paramagnetic
resonance (EPR), and small-angle X-ray scattering (SAXS) on recombinantly
produced, “healthy” charge variants rmC1WT and double
cysteine variant C1S17CH85C, we find that the size and the shape of
the determined nanostructures in an optimum mixture offer model membranes
in which the protein exhibits native behavior. SAXS measurements illuminate
the size and shape of the nanostructures and indicate IL-rich “beads”
clipped together by functional MBP, one of the in vivo roles of the
protein in the myelin sheath. All the gathered data combined indicate
that the 50% and 45% aqueous IL mixtures can be described as offering
minimal models of a lipid mono- or bilayer that allow native processing
and potential study of at least peripheral membrane proteins like
MBP.