Protein Unfolding, and the “Tuning In” of Reversible Intermediate States, in Protic Ionic Liquid Media

Byrne, Nolene; Angell, C. Austen

doi:10.1016/j.jmb.2008.02.050

Cited by 119 publications

(126 citation statements)

References 33 publications

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“…31,32 It is not clear, whether these peaks reflect on-pathway species in the normal unfolding process or misfolds. As noted by Byrne and Angell, 45,46 the right solvent environment, in their case created by highly concentrated hydrophilic ILs, stabilizes such conformations.…”

Section: Effects Of Ionic Liquids On Non-native Protein Aggregationmentioning

confidence: 91%

“…4,8,15,16 Solvent modification can stabilize or destabilize the native fold, [27][28][29][30][31][32][33][34] enhance refolding, 42,43 optimize protein crystallization, 44 disrupt aggregates, 32 or steer the formation of intermediates. 32,45,46 The literature contains many useful, but more-or-less empirical guide lines for solvent optimization. 4,8,15,16 Rational strategies for solvent optimization require their molecular understanding.…”

Section: -24mentioning

confidence: 99%

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How ionic liquids can help to stabilize native proteins

Weingärtner

Cabrele

Herrmann

2012

Phys. Chem. Chem. Phys.

260

233

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The native state of a globular protein is essential for its biocatalytic function, but is marginally stable against unfolding. While unfolding equilibria are often reversible, folding intermediates and misfolds can promote irreversible protein aggregation into amorphous precipitates or highly ordered amyloid states. Addition of ionic liquids-low-melting organic salts-offers intriguing prospects for stabilizing native proteins and their enzymatic function against these deactivating reaction channels. The huge number of cations and anions that form ionic liquids allows fine-tuning of their solvent properties, which offers robust and efficient strategies for solvent optimization. Going beyond case-by-case studies, this article aims at discussing principles for a rational design of ionic liquid-based formulations in protein chemistry and biocatalysis.

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Section: Effects Of Ionic Liquids On Non-native Protein Aggregationmentioning

confidence: 91%

Section: -24mentioning

confidence: 99%

How ionic liquids can help to stabilize native proteins

Weingärtner

Cabrele

Herrmann

2012

Phys. Chem. Chem. Phys.

260

233

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“…(i) Kill bacteria (O'Toole et al 2012); (ii) Extract, purify, and even store DNA at ambient temperature (Clark et al 2015(Clark et al , 2016; (iii) Stabilize proteins and enzymes Venkatesu 2014, Kumar et al 2017); (iv) Assist or prevent protein amyloidogenesis, and in some cases even return amyloid fibers to functional proteins (Byrne et al 2007, Byrne and Angell 2008, 2009);…”

Section: Introductionmentioning

confidence: 99%

“…Multi-lamellar structures can also be formed Fig. 1 Chemical sketches of some selected RTILs cations: (a),(b),(c) the most common imidazolium and pyrridinium RTIL cations; (d),(e) the doubletail lipid-mimic imidazoliumbased RTILs (Wang et al 2015a); (f),(g) the ethylammonium and guanidinium RTIL cations that help and contrast protein amyloidogenesis, respectively (Byrne et al 2007, Byrne and Angell 2008, 2009); (h) a phosphonium-based RTIL cation; and (i),(l) the choline and phosphocholine cations also used in RTILs made of amino acids (Benedetto et al 2014a) between RTILs and model biomembranes. Their aim is to determine the microscopic mechanisms behind their observed biological effects.…”

Section: Introductionmentioning

confidence: 99%

Room-temperature ionic liquids meet bio-membranes: the state-of-the-art

Benedetto

2017

Biophys Rev

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Room-temperature ionic liquids (RTIL) are a new class of organic salts whose melting temperature falls below the conventional limit of 100°C. Their low vapor pressure, moreover, has made these ionic compounds the solvents of choice of the so-called green chemistry. For these and other peculiar characteristics, they are increasingly used in industrial applications. However, studies of their interaction with living organisms have highlighted mild to severe health hazards. Since their cytotoxicity shows a positive correlation with their lipophilicity, several chemical-physical studies of their interactions with biomembranes have been carried out in the last few years, aiming to identify the molecular mechanisms behind their toxicity. Cation chain length and anion nature of RTILs have seemed to affect lipophilicity and, in turn, their toxicity. However, the emerging picture raises new questions, points to the need to assess toxicity on a case-by-case basis, but also suggests a potential positive role of RTILs in pharmacology, bio-medicine and bio-nanotechnology. Here, we review this new subject of research, and comment on the future and the potential importance of this emerging field of study.

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“…In particular the lengthening of the alkyl chain seems to have a positive effect on dissolving the aggregates and a negative effect on refolding the protein. 16,17,18,19 In the last years the effects of ILs on several proteins have been extensively investigated by varying ILs composition (anion, cation, and alkyl chains) and denaturing conditions up to fibrillar aggregates. 20,21,22 Many interesting studies on the ILs-protein interaction have been carried out on lysozyme ( Fig.…”

mentioning

confidence: 99%

Role of ionic liquids in protein refolding: native/fibrillar versus treated lysozyme

et al. 2012

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Several ionic liquids (ILs) are known to revert aggregation processes and improve the in vitro refolding of denatured proteins. In this paper the capacity of a particular class of ammonium based ILs to act as refolding enhancers was tested using lysozyme as a model protein. Raman spectra of ILs treated fibrillar lysozyme as well as lysozyme in its native and fibrillar conformations were collected and carefully analyzed to characterize the refolding extent under the effect of the IL interaction. Results obtained confirm and largely extend the earlier knowledge on this class of protic ILs and indicate Ethyl Ammonium Nitrate (EAN) as the most promising additive for protein refolding. The experiment provides also the demonstration of the high potentiality of Raman spectroscopy as a comprehensive diagnostic tool in this field. IntroductionProtein aggregation is one of the most important problems in the production and storage industrial processes and therefore among the causes of the major economic loss in biotechnology and pharmaceutical factories. Indeed in manufacturing commercial products, the goal is to obtain a stable and correct protein folding for allowing the full functionality. 1 The problems of protein aggregation and structural stability are not limited to the manufacturing processes. Protein misfolding diseases are a well-known class of ailments including Alzheimer, Parkinson and Huntington diseases. They all involve protein aggregation and share common features such as the presence of insoluble fibrous protein aggregation in a specific structural motif characterized by a cross-β sheet structure. 2 Key issues on aggregation are not yet fully addressed such as the detailed microscopic mechanism leading to aggregation, the structure of aggregates, how the environmental conditions can affect the rate and the amount of aggregation and how aggregation can be prevented and/or removed. Additives may promote the stabilization of the native state of the protein accelerating the kinetics of the correct folding and removing/inhibiting the aggregation of denatured polypeptides and intermediates of the folding pathways. 3In recent years ionic liquids (ILs) have been used to stabilize the protein activity, to inhibit or reduce aggregation, and to improve the in vitro refolding of denatured proteins. 4,5 ILs have numerous attractive characteristics including their non-volatility, good solvating properties, thermal stability, and recyclability, that render these compounds "environmentally green". 6,7,8,9,10 One of the most important qualities of these solvents is the high tunability of their chemical structure. Indeed, they can be designed to have specific physical and chemical qualities by acting on either the alkyl chains (i.e. modifying the length, the presence of hydrophobic groups, etc.) or the anion (i.e. varying the degree of the charge delocalization, its hydrogen bonding ability, etc). 11 ILs having coordinating anions which are strong hydrogen bond acceptors (e.g. Cl − , NO 3 − , CH 3 COO − and (MeO) 2 PO 2 − )...

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Protein Unfolding, and the “Tuning In” of Reversible Intermediate States, in Protic Ionic Liquid Media

Cited by 119 publications

References 33 publications

How ionic liquids can help to stabilize native proteins

How ionic liquids can help to stabilize native proteins

Room-temperature ionic liquids meet bio-membranes: the state-of-the-art

Role of ionic liquids in protein refolding: native/fibrillar versus treated lysozyme

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