Understanding ethylammonium nitrate stabilized cytochrome c – Molecular dynamics and experimental approach

Jaganathan, Maheshkumar; Velmurugan, D.; Dhathathreyan, Aruna

doi:10.1016/j.molstruc.2014.10.049

Cited by 34 publications

(32 citation statements)

References 57 publications

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“…86 This solvophobic force 87 compels the alkyl group to cluster in apolar domains. The above interaction mechanism suggested by Jaganathan et al 85 is consistent with sponge like structure of EAN with alternating layers of non-polar and charged regions as suggested by X-ray reflectivity studies by Niga et al 86 Therefore, the organized assembly of EAN around the hydrated protein is providing stability to the protein.…”

Section: The Role Of Ammonium-based Ils On the Stability Of Heme Protsupporting

confidence: 70%

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

Jha

Venkatesu

2015

Phys. Chem. Chem. Phys.

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The large amount of attention earned by ionic liquids (ILs) in the various physical and chemical sciences has been attributed to their unique, designer nature. In the past few years, the role of ILs in protein folding/unfolding has been rapidly growing. In light of the increasing importance of ILs, it is desirable to systematize the ion effects on protein properties such as structure stability, activity and enantioselectivity. Various studies available in the literature show ILs as a potential solvent medium for many enzymatic reactions, as well as in various protein folding/unfolding studies. Various reviews by many researchers focus on the synthesis, application and general properties of the ILs, however a review focussing on the effect of various ILs on the activity, structure and stability of proteins is still missing. Also, according to the best of our knowledge there is no single review available throughout the literature that focuses on the effect of the same family of ILs on different proteins. Therefore, it is a priority to obtain complete knowledge of the biomolecules, particularly amino acids (AAs) and proteins in a particular IL family. The focus of the present perspective is to investigate the performance of a list of proteins and protein model compounds in the presence of ammonium-based ILs. This perspective presents a survey of all the key developments from the available reports and also our past and present experience related to proteins and ammonium-based ILs. Additionally, we have tried to put the available information in chronological order in most of the cases. The use of ammonium family ILs as a co-solvent for various proteins model compounds and proteins has been outlined. This perspective can act as a barometer for reckoning the various advancements made in this field and can also galvanize further investigation of various untouched aspects of this research area.

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Section: The Role Of Ammonium-based Ils On the Stability Of Heme Protsupporting

confidence: 70%

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

Jha

Venkatesu

2015

Phys. Chem. Chem. Phys.

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“…40 Among other important biomolecules, the critical importance of alkylammonium formates and nitrates in the stabilization of cytochrome c has also been explored rigorously using both spectroscopic techniques 41 as well as MD simulations. 42 Alkylimidazolium acetates have also been used as a pretreatment solvent for extracting lignin from wood by Lee et al 43 Alkylammonium based ionic liquids, on the other hand, have been shown to exhibit a strong positive effect on the conservation of haemoglobin structure by Attri et al 44 In an important work, Attri et al have shown that triethylammonium acetate (TEAA), a protic ionic liquid can counteract the deleterious effects of urea on the biologically relevant enzyme a-chymotrypsin using circular dichroism (CD) and NMR techniques. 45 They have shown that TEAA can effectively offset the harsh action of urea even when its relative concentration is as low as 1 : 5 with respect to the denaturant urea.…”

Section: Introductionmentioning

confidence: 99%

Ammonium based stabilizers effectively counteract urea-induced denaturation in a small protein: insights from molecular dynamics simulations

Sarkar

Ghosh

2017

RSC Adv.

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“…The effect of EAN on renaturation of cyt c has been shown by Jaganathan et al [140] and the results show that EAN in the range of 10 −4 M helps in refolding of the protein from urea (8 M)-induced denaturation of cyt c. On the other hand, it was observed that at moderate concentrations ( 4 ] anion. Moreover, it is interesting to note that some of the imidazolium-based ILs could be used as anticancer solvents [142].…”

Section: Very Recently At Low Concentration Of [Bmim][cl]mentioning

confidence: 83%

“…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].…”

mentioning

confidence: 99%

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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Understanding ethylammonium nitrate stabilized cytochrome c – Molecular dynamics and experimental approach

Cited by 34 publications

References 57 publications

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

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

Ammonium based stabilizers effectively counteract urea-induced denaturation in a small protein: insights from molecular dynamics simulations

The Role of Ionic Liquids in Protein Folding/Unfolding Studies

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