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

Jha, Indrani; Venkatesu, Pannuru

doi:10.1021/acssuschemeng.5b00939

Cited by 45 publications

(45 citation statements)

References 57 publications

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“…The addition of ionic liquids (ILs), which have emerged as a promising solvent, strengthen the stability of biomolecules like proteins, enzymes and DNA . Recent studies have shown that ILs can influence the protein activity and stability, improve refolding, and inhibit the aggregation …”

Section: Introductionmentioning

confidence: 99%

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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Section: Introductionmentioning

confidence: 99%

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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“…In recent decades, it has been observed that selected ILs are able: (1) to kill bacteria and cancer cells while leaving eukaryotic healthy cells almost unaffected; (2) to extract, purify and even preserve DNA at ambient temperature; (3) to stabilize proteins and enzymes; (4) to either favour or prevent protein amyloidogenesis; (5) to penetrate and eventually disrupt biomembranes via extended poration; and (6) to dissolve polysaccharides and cellulose. A recent overview of the subject is reported in two reviews authored by Benedetto and Ballone (2016a, b).The aim of the BIonic Liquid meet Biomolecules^session of the IUPAB-EBSA congress was to present an up-to-date overview of this new and intriguing subject of research which has potential applications in several fields, ranging from biomedicine, pharmacology, and material science to bionanotechnologies.Pannuru Venkatesu (University of Delhi, India) focuses on the interaction between ionic liquids and proteins (Meena et al 2016;Jha and Venkatesu 2016), arguing that studies of interaction between proteins and different ILs in aqueous solution are comparatively more important than those in pure ILs. The results of these investigations suggest that the ILwater-protein interaction is a complex balance of different contributions by the different components, which is not possible to predict a priori.…”

mentioning

confidence: 99%

“…Pannuru Venkatesu (University of Delhi, India) focuses on the interaction between ionic liquids and proteins (Meena et al 2016;Jha and Venkatesu 2016), arguing that studies of interaction between proteins and different ILs in aqueous solution are comparatively more important than those in pure ILs. The results of these investigations suggest that the ILwater-protein interaction is a complex balance of different contributions by the different components, which is not possible to predict a priori.…”

mentioning

confidence: 99%

Overview of the “Ionic Liquids meet Biomolecules” session at the 19th international IUPAB and 11th EBSA congress

Benedetto

Galla

2017

Biophys Rev

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Room temperature ionic liquids (ILs) (Welton 1999) are a vast class of ionic systems consisting of an organic cation and either an organic or inorganic anion, whose melting temperature falls below the conventional limit of 100°C, making these compounds liquid at or near room temperature. The thermal and chemical stability of these systems make them the basis of what is called Bgreen chemistry^ (Earle and Seddon 2000). Several biochemical studies, however, have highlighted their potential toxicity to organisms, a toxicity which, in turn, is also a measure of their affinity for bio-molecules. This property has stimulated several chemical-physical studies on the interaction between ILs and basic biological systems. In recent decades, it has been observed that selected ILs are able: (1) to kill bacteria and cancer cells while leaving eukaryotic healthy cells almost unaffected; (2) to extract, purify and even preserve DNA at ambient temperature; (3) to stabilize proteins and enzymes; (4) to either favour or prevent protein amyloidogenesis; (5) to penetrate and eventually disrupt biomembranes via extended poration; and (6) to dissolve polysaccharides and cellulose. A recent overview of the subject is reported in two reviews authored by Benedetto and Ballone (2016a, b).The aim of the BIonic Liquid meet Biomolecules^session of the IUPAB-EBSA congress was to present an up-to-date overview of this new and intriguing subject of research which has potential applications in several fields, ranging from biomedicine, pharmacology, and material science to bionanotechnologies.Pannuru Venkatesu (University of Delhi, India) focuses on the interaction between ionic liquids and proteins (Meena et al. 2016;Jha and Venkatesu 2016), arguing that studies of interaction between proteins and different ILs in aqueous solution are comparatively more important than those in pure ILs. The results of these investigations suggest that the ILwater-protein interaction is a complex balance of different contributions by the different components, which is not possible to predict a priori. There is sufficient evidence in the literature to lead to the conclusion that the interaction between proteins and ILs depends on the protein as well as on the cations and anions present in the ILs.Antonio Benedetto (University College Dublin, Ireland, and Paul Scherrer Institut, Switzerland) presents results from joint experimental and computational studies on the interaction between ILs and (model) biomembranes (Benedetto 2017;Benedetto et al. 2015, Benedetto et al. 2014. Combining neutron scattering and computer simulations these studies show how it is possible to describe the mechanisms of interaction at the molecular level: IL cations penetrate the biomembrane, finding a preferential location between the tails and the heads of the phospholipids. The penetration is driven by the Coulombic attraction between the IL cations and one of the most electronegative oxygen atoms in the phospholipid heads, and is stabilized by dispersion forces between the lipids and th...

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“…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 contrasting nature of ammonium family ILs is also consistent with Rodrigues et al[151], where among different families of ILs only ammonium-containing IL shows higher activity as compared to imidazolium-based ILs for Thermomyces lanuginosus lipase (TlL). Scheme 2 shows the difference between the biocompability behaviors of ammonium-and imidazolium-based ILs.On the other hand, Jha et al[152] have explored the influence of a of imidazolium-based IL, 1-allyl-3-methylimidazolium chloride ([Amim][Cl]), on the stability of Hb. Unprecedented improvement in the stability of Hb in the presence of [Amim][Cl] at the lower concentration of [Amim][Cl] was…”

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

Cited by 45 publications

References 57 publications

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

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

Overview of the “Ionic Liquids meet Biomolecules” session at the 19th international IUPAB and 11th EBSA congress

The Role of Ionic Liquids in Protein Folding/Unfolding Studies

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