Endeavour to simplify the frustrated concept of protein-ammonium family ionic liquid interactions

Jha, Indrani; Venkatesu, Pannuru

doi:10.1039/c5cp01735a

Cited by 59 publications

(45 citation statements)

References 140 publications

(319 reference statements)

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“…[19][20][21][22][23] Studies have shown ammonium-based ILs to act as better stabilizing agent for proteins as compared to imidazolium-based ILs. 24 Our research group has out carried protein stability studies in both ammonium and imidazolium-based ILs. 16,[25][26][27][28][29] Recently, Jha et al 27 showed the destabilization of Mb and Hb in ammonium-based ILs which was much unexpected result because of the fact that ammonium-based ILs are known as good protein stabilizers.…”

Section: Introductionmentioning

confidence: 99%

Unprecedented Improvement in the Stability of Hemoglobin in the Presence of Promising Green Solvent 1-Allyl-3-methylimidazolium Chloride

Jha

Venkatesu

2015

ACS Sustainable Chem. Eng.

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In this article, we have explored the influence of peculiar member of imidazolium-based ionic liquid (IL) 1-allyl-3-methylimidazolium chloride ([Amim][Cl]) on the stability of haemoglobin (Hb) by using fluorescence, thermal fluorescence, ANS fluorescence, circular dichroism (CD) spectroscopy and dynamic light scattering (DLS) measurements. In the attempt of searching of IL which can provide stability to Hb, for the first time, we have successfully shown the stability of Hb in [Amim][Cl]. Our results show that [Amim][Cl] stabilizes the Hb native structure in concentration dependent manner which indicates to fact that the concentration of IL is very crucial to determine the stabilization/destabilization of the protein in ILs. Here, we have observed that low concentration of IL provides stability to the protein while high concentration destabilizes the protein. The commendatory results obtained from the multi spectroscopic approaches provided some guidance regarding the mechanism of interaction between Hb and [Amim][Cl]. The predicted mechanism may be the accumulation of imidazolium cation on the protein surface and tendency of anion to remain in the bulk phase ultimately resulting in stabilization of the protein since; this can in direct/indirect way affect the hydrogen bonding of protein with the surrounding water. on the basis of our results [Amim][Cl] seems to be novel solvent for the stability of Hb, however, further studies with other proteins need to be carried out for further information. CONCLUSION Our results illustrate that interactions of ions of ILs with proteins are important for understanding the effects shown by them on proteins whether stabilization/destabilization. These interactions are governed by the ions present as well as the concentrations used. In this work [Amim][Cl] has been identified as a compatible solvent for Hb structure, nevertheless, the stabilization tendency being concentration dependent. Low concentration of [Amim][Cl] stabilized Hb while higher concentration destabilized Hb. Therefore, the results obtained here facilitate a much better understanding of protein folding/unfolding in IL. Hence, this IL was found to be stabilizing agent for Hb. Since, [Amim][Cl] is thermally stable as well as non-volatile, consequently it can be supposed to be promising green/biocompatible solvent for the proteins. However, further research with other proteins in the presence of this IL is required. Also, from our research this becomes completely clear that the role of alkyl group of imidazolium ILs is vital in determining the protein stability. Therefore, this work can encourage designing of novel ILs which can provide stability to many other proteins. ASSOCIATED CONTENT Supporting InformationThe supporting information is available free of charge on the ACS Publications website Thermal fluorescence spectra analysis of the Hb in buffer and in different concentrations of [Amim][Cl] (Figures S1-S7). Synopsis: The native structure of Hb concentration of [Amim][Cl] Graphical AbstractUnprecedented Improv...

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Section: Introductionmentioning

confidence: 99%

Unprecedented Improvement in the Stability of Hemoglobin in the Presence of Promising Green Solvent 1-Allyl-3-methylimidazolium Chloride

Jha

Venkatesu

2015

ACS Sustainable Chem. Eng.

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“…These unique properties of ILs make them very attractive nonaqueous solvents for protein stability studies. It is revealed from various studies that physicochemical properties of ILs can play a pivotal role in altering the structure, stability and activity of proteins/enzymes [44]. Moreover, ILs offer new possibilities of application of solvent engineering to enzymatic reactions.…”

Section: Protein Stability In the Presence Of Ilsmentioning

confidence: 99%

“…Studies carried out by various groups using CT suggest that the physical properties of ILs such as polarity and hydrophobicity play a major role in their stabilizing behavior toward CT [18,52,53]. Among various families of ILs, ammonium-based ILs are identified to display their wide range application in biochemical processes [44].…”

Section: Protein Stability In the Presence Of Ilsmentioning

confidence: 99%

“…This will not only increase the shelf life of insulin, whereas suitable formulations of insulin in biocompatible ILs can lead to safe and durable insulin formulations in pharmaceutical products. The ammonium-based ILs such as ethylammonium mesylate (EaM), diethylammonium mesylate (DeaM)-stabilized tobacco mosaic virus, whereas triethylammonium mesylate (TeaM) caused a change in the secondary structure of the virus[149].From the literature and from our own experience, it can be suggested that ammonium-based ILs are more biocompatible as compared to the imidazolium-based ILs[44,[140][141][142][143][144][145][146][147][148][149][150][151][152][153][154][155]. Yu et al [150] explored the stability of laccase in the presence of both ammonium-and imidazolium-based ILs such as [TMA][TfO], [Bmim][TfO] and [Bmpyr][TfO].…”

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“…Scheme 2. The biocompatible behavior of ammonium-based ILs as compared to imidazolium-based ILs for proteins (Ref [44]…”

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The Role of Ionic Liquids in Protein Folding/Unfolding Studies

Kumar¹,

Bisht²,

Jha³

et al. 2017

Progress and Developments in Ionic Liquids

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Ionic liquids (ILs) have emerged as novel solvent medium for several biotechnological processes in vitro. The use of ILs starts from protein extraction to catalysis to folding/ unfolding studies. ILs are becoming the most favorite non-aqueous medium for protein studies due to their unique ionic combinations (cation + anion) and tunable physical properties. In this context, several research results have been published that use of pure or aqueous IL solutions as stabilizer for proteins. Hence, herein, in this chapter, we present a collection of research work that focuses on the importance of ILs (and their mixture) in protein stabilities. In addition, we have also reviewed the unique properties of ILs as counteracting solvents for cold-induced denaturation and also their refolding properties. This report will definitely generate a new understanding for the ILs, their importance and applicability in protein folding studies.that is now considered as the first IL is ethylammonium nitrate ([C 2 H 5 NH 3 ][NO 3 ], EAN) and was prepared by Paul Walden in 1914 and has a melting point of 12°C [8]. After a long gap, the major studies of room temperature molten salts of pyridinium halides with aluminum chloride (AlCl 3 ) were made in the 1940s by a group led by Frank Hurley and Tom Weir at Rice University [9]. Later, alkylimidazolium salts (C n mim) + were also reported in the early 1980s [10]. An excellent short history of the birth of ILs, which covers the crucial moments of this area, is presented by John S. Wilkes [11].In its initial revolutionary stage, ILs were vastly considered in analytical chemistry based on their unique and tunable physical properties. Since then, synthesis of a large number of multifunctional ILs has been a prime interest for synthetic chemists [12,13]. In this context, varieties of task-specific ILs have been synthesized and the advantages of their physical properties have been reported in an open literature [14]. Common ILs include ammonium, phosphonium, sulfonium, guanidinium, pyridinium, imidazolium and pyrrolidinium cations. The most common anions are chloride, bromide, tetrafluoroborate, hexafluorophosphate, trifluoromethanesulfonyl, bis(trifluoromethanesulfonyl)imide, dicyanamide and alkyl sulfate anions. These ILs have some unique properties such as negligible vapor pressure, good thermal stability, tunable viscosity and miscibility with water, a wide electrochemical window, high conductivity and high heat capacity [15][16][17]. These physical properties make IL a promising material in numerous fields, for example, their use in electrochemical devices and replacements for several organic reactions [18,19]. Gordon [20], Parvulescu and Hardacre [21] and Crowhurst et al. [22] pointed out that there is an obvious advantage in performing many reactions in ILs due to the improvement in reaction activity, selectivity and yield. An in-depth literature survey reveals that there tremendously exist a large number of scholarly articles as well as elegant reviews that explicitly elucidate the various s...

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Comprehensive Evaluation of Biomolecular Interactions between Protein and Amino Acid Based‐Ionic Liquids: A Comparable Study between [Bmim][Br] and [Bmim][Gly] Ionic Liquids

2016

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Protein is one of the most intricate and overriding biological system. Over the past years, there is an increased demand to consider ionic liquids (ILs) as novel biocompatible co-solvents for proteins.The overwhelming attention grabbed by new-generation ''amino acid ionic liquids (AAILs)''among various fields of modern chemistry and biology, has been attributed to their unique and designer nature. However, the stability of proteins in such AAILs is still untouched. Therefore, we have synthesized 1-butyl-3-methylimidazolium glycine ([Bmim][Gly]) in which anion is directly derived from natural amino acid and characterized to improve the stability of stem bromelain (BM). Since, it is speculated that replacement of cation/anion with the amino acids (AAs) will improve the stability of protein. Therefore, the main aim of present work is to highlight the influence of [Bmim][Gly] on the conformational stability and activity of BM. Furthermore, enzyme's stability and activity arecompared with the conventional imidazolium-based ionic liquid i. e. 1-butyl-3methylimidazolium bromide [Bmim][Br] by using spectroscopic techniques, enzyme assay and molecular docking. Our study shows that both studied ILs interact with functional groups of BM. As a result, in contrast to our expectation it appears that [Bmim] [Br] stabilizes BM more than [Bmim] [Gly]. We believe that present study will provide new insights into the interactions between enzyme and AAILs in the field of protein stabilization.

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Endeavour to simplify the frustrated concept of protein-ammonium family ionic liquid interactions

Cited by 59 publications

References 140 publications

Unprecedented Improvement in the Stability of Hemoglobin in the Presence of Promising Green Solvent 1-Allyl-3-methylimidazolium Chloride

Unprecedented Improvement in the Stability of Hemoglobin in the Presence of Promising Green Solvent 1-Allyl-3-methylimidazolium Chloride

The Role of Ionic Liquids in Protein Folding/Unfolding Studies

Comprehensive Evaluation of Biomolecular Interactions between Protein and Amino Acid Based‐Ionic Liquids: A Comparable Study between [Bmim][Br] and [Bmim][Gly] Ionic Liquids

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