2012
DOI: 10.1016/j.jlumin.2011.10.026
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Interaction mechanisms of ionic liquids [Cnmim]Br (n=4, 6, 8, 10) with bovine serum albumin

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Cited by 82 publications
(55 citation statements)
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“…This confirms the conclusion that imidazolium surfactants interact with BSA more strongly than quaternary ammonium surfactants with the same hydrophobic chain. The explanations may be that imidazolium surfactants display the strong p-p interaction, namely, the aromatic ring stacking between the imidazolium rings and the residues (such as Trp, Tyr, and Phe) in BSA, besides electrostatic and hydrophobic interactions [39,40,47], attributing to the existence of aromatic functional groups imidazolium ions for [C n -4-C n im]Br 2 or [C 12 mim]Br. This aromatic ring stacking leads to the more expanding of polypeptide and the larger unfolding of BSA.…”
Section: Resultsmentioning
confidence: 99%
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“…This confirms the conclusion that imidazolium surfactants interact with BSA more strongly than quaternary ammonium surfactants with the same hydrophobic chain. The explanations may be that imidazolium surfactants display the strong p-p interaction, namely, the aromatic ring stacking between the imidazolium rings and the residues (such as Trp, Tyr, and Phe) in BSA, besides electrostatic and hydrophobic interactions [39,40,47], attributing to the existence of aromatic functional groups imidazolium ions for [C n -4-C n im]Br 2 or [C 12 mim]Br. This aromatic ring stacking leads to the more expanding of polypeptide and the larger unfolding of BSA.…”
Section: Resultsmentioning
confidence: 99%
“…Compared with conventional surfactants, they have a number of unique properties [45], such as lower critical micelle concentration (cmc), higher adsorption efficiency, and better wetting property. Moreover, examining a wide range of surfactants with various head groups and different numbers of hydrophobic alkyl chains, such as dicationic quaternary ammonium compounds [39,41,42,44] or the cationic imidazolium surfactant [47], could get a systematic understanding about the role of surfactants' structures in the interaction of protein/surfactant. Mir et al [42] have studied the effect of spacer length and the hydrophobic counterpart of gemini homologues (C 16 C s C 16 Br 2 , s = 4, 5, 6) on the interaction of BSA, and the results showed that the gemini surfactants interact more efficiently with the proteins than their conventional single chain counterparts and their efficiencies increase with decrease in the length of spacer.…”
Section: Introductionmentioning
confidence: 99%
“…They possess two main characteristics that qualify them as promising alternatives to classical (toxic) solvents: i) negligible vapour pressures in a wide temperature range [2,3] thus providing low atmospheric pollution and ii) diverse solvent power -they dissolve well a number of both polar and non-polar solutes, as it was reported [4] and reviewed in literature [5,6]. Therefore, ionic liquids found their applications as separation/extraction solvents for diverse solutes: for amino acids separation and purification [7][8][9], carbohydrate separation [10], for extraction of proteins [11], phenols [12], azo dyes [13], or for removal of free fatty acids [14].…”
Section: Introductionmentioning
confidence: 99%
“…These changes also explain the deformation of peptide bond. The close and ordered peptide chain changes in to the loose and disordered chain [27].…”
Section: Ultraviolet Spectramentioning
confidence: 99%
“…These changes also explain the deformation of peptide bond. The close and ordered peptide chain changes in to the loose and disordered chain [27].The change in absorbance on addition of cationic amphiphiles also indicated that the cationic head groups of the amphiphiles bind to amino acid residues via H-bond. In case of single tailed amphiphiles, a gradual blue shift of maximum wavelength confirmed the interaction and unfolding of BSA, which transferred the BSA towards more hydrophobic region (Figures 5c and 5d).…”
mentioning
confidence: 99%