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

Singh, Upendra Kumar; Dohare, Neeraj; Mishra, Prabhash; Singh, Prashant; Bohidar, H. B.; Patel, Rajan

doi:10.1016/j.jphotobiol.2015.04.011

Cited by 32 publications

(15 citation statements)

References 58 publications

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“…Lifetime measurements gather valuable information about conformational multifariousness of proteins. The folding/unfolding conditions prevailed largely due to the extent of solvent accessibility, and several local configurations of proteins determine the contribution of respective components . Interaction of Trp residues in protein with the local environment and the solvent assimilates to provide the fluorescence lifetime.…”

Section: Resultsmentioning

confidence: 99%

Esterase activity and conformational changes of bovine serum albumin toward interaction with mephedrone: Spectroscopic and computational studies

Patel

Maurya

Parray

et al. 2018

J of Molecular Recognition

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The present work is a brief overview of the effect of psychostimulant drug mephedrone hydrochloride (4MMC) on a transport protein, bovine serum albumin (BSA). The binding effect of 4MMC on BSA has been investigated by using UV-visible, steady-state fluorescence, time-resolved fluorescence, fluorescence resonance energy transfer, Fourier transform infrared, circular dichroism, and molecular docking method. 4-Methylmephedrone quenched the intrinsic fluorescence of BSA by static quenching mechanism, which was further confirmed by time-resolved fluorescence. The absorption spectrum of BSA in the presence of various concentrations of 4MMC reveals the change in the absorption bands of BSA-4MMC complex. The binding constant between 4MMC and BSA was calculated to be of the order of 10 Lmol . The thermodynamic parameters such as molar enthalpy change (∆H), molar Gibbs free energy change (∆G), and molar entropy contribution (∆S) were obtained by the van't Hoff equation. The values obtained suggested that the binding mechanism was entropic driven and the major forces involved are hydrophobic in nature. The fluorescence resonance energy transfer result indicates the high probability of energy transfer from Trp residue of BSA to the 4MMC (r = 2.01 nm). Fourier transform infrared and CD results showed that 4MMC induced secondary structural changes in BSA. The esterase-like activity of BSA in presence of 4MMC further validated our CD results, confirming the distortion and change in functionality of protein upon binding with 4MMC. Molecular docking analysis showed that 4MMC principally bind at the II site (subdomain IIIA) of BSA.

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Section: Resultsmentioning

confidence: 99%

Esterase activity and conformational changes of bovine serum albumin toward interaction with mephedrone: Spectroscopic and computational studies

Patel

Maurya

Parray

et al. 2018

J of Molecular Recognition

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“…The interactions between ILs in aqueous solution and lipid bilayer membranes have guided the development of IL-based drug formulation and drug-delivery applications [10,11,12,13,14,15,16,17,18,19,20] and opened research avenues for IL-based antibiotics and antibiotic-IL combinations. There have also been several reports highlighting both experimental and computational studies on how ILs interact with lipid bilayers [21,22].…”

Section: Introductionmentioning

confidence: 99%

Correlating Lipid Membrane Permeabilities of Imidazolium Ionic Liquids with Their Cytotoxicities on Yeast, Bacterial, and Mammalian Cells

et al. 2019

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Alkyl-imidazolium chloride ionic liquids (ILs) have been broadly studied for biochemical and biomedical technologies. They can permeabilize lipid bilayer membranes and have cytotoxic effects, which makes them targets for drug delivery biomaterials. We assessed the lipid-membrane permeabilities of ILs with increasing alkyl chain lengths from ethyl to octyl groups on large unilamellar vesicles using a trapped-fluorophore fluorescence lifetime-based leakage experiment. Only the most hydrophobic IL, with the octyl chain, permeabilizes vesicles, and the concentration required for permeabilization corresponds to its critical micelle concentration. To correlate the model vesicle studies with biological cells, we quantified the IL permeabilities and cytotoxicities on different cell lines including bacterial, yeast, and ovine blood cells. The IL permeabilities on vesicles strongly correlate with permeabilities and minimum inhibitory concentrations on biological cells. Despite exhibiting a broad range of lipid compositions, the ILs appear to have similar effects on the vesicles and cell membranes.

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“…The quest for liquids that possess such fascinating properties of molecular liquids and provide a unique possibility to modulate protein stability, a reason for this burst of interest includes their widely tunable properties. ,,− The different interaction behavior of ILs with proteins has long been reported in neat IL and ILs in aqueous medium. , Significant advances in the ability of ILs to impart stability to proteins and ultimately conserve their structure have been made. ,,,− A few ILs have been reported as having an outstanding ability to stabilize proteins over time and high temperature. ,,, A study by Bihari et al showed that the presence of neat IL alters the tertiary structure of h-cyt c ; however, it was not accompanied by aggregation of the protein . Recently, a fascinating study of newly synthesized protein–polymer surfactant nanoconstructs reported by Alex et al imparts high thermal stability to protein .…”

Section: Introductionmentioning

confidence: 99%

Mechanism and Dynamics of Long-Term Stability of Cytochrome c Conferred by Long-Chain Imidazolium Ionic Liquids at Low Concentration

Singh

Kumari

Khan

et al. 2017

ACS Sustainable Chem. Eng.

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

Cited by 32 publications

References 58 publications

Esterase activity and conformational changes of bovine serum albumin toward interaction with mephedrone: Spectroscopic and computational studies

Esterase activity and conformational changes of bovine serum albumin toward interaction with mephedrone: Spectroscopic and computational studies

Correlating Lipid Membrane Permeabilities of Imidazolium Ionic Liquids with Their Cytotoxicities on Yeast, Bacterial, and Mammalian Cells

Mechanism and Dynamics of Long-Term Stability of Cytochrome c Conferred by Long-Chain Imidazolium Ionic Liquids at Low Concentration

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