Effect of pyrrolidinium based ionic liquid on the channel form of gramicidin in lipid vesicles

[Display omitted] •CD spectrum of membrane bound gramicidin is sensitive to the conformational changes with the addition of BMOP.•REES suggests possible interactions of BMOP with channel form gramicidin in vesicle.•Surface activity of the gramicidin in vesicle is more with BMOP.•BMOP forms a film around the membrane bound gramicidin. The present work is focused on the interaction between membrane bound gramicidin and 1-butyl-1-methyl-2-oxopyrrolidinium bromide (BMOP) ionic liquid. Ionic liquids (ILs) are solvents that are often liquid at room temperature and composed of organic cation and appropriate anion. The gramicidin peptide forms prototypical ion channels for cations, which have been extensively used to study the organization, dynamics, and function of membrane spanning channels. The interaction was studied by circular dichroism, steady state, time-resolved fluorescence spectroscopy in combination with dynamic surface tension and field emission scanning electron microscopic methods (FESEM). The results obtained from circular dichroism shows that the BMOP interacts with the channel form of gramicidin in lipid vesicle without any considerable effect on its conformation. The Red-edge excitation shift (REES) also supported the above findings. In addition, the fluorescence studies suggested that BMOP makes ground state complex with ion channel, which was further supported by time resolved measurements. Furthermore, dynamic surface tension analysis shows the faster adsorption of BMOP with membrane bound gramicidin at the air–water interface. Additionally, FESEM results indicated that BMOP forms a film around the membrane bound gramicidin at higher concentration. These results are potentially useful to analyze the effect of ionic liquids on the behaviour of membrane proteins.