Ionic Liquid-Induced Formation of the α-Helical Structure of β-Lactoglobulin

Takekiyo, Takahiro; Koyama, Yoshihiro; Yamazaki, Katsumi; Abe, Hiroshi; Yoshimura, Yukihiro

doi:10.1021/jp405834n

Cited by 43 publications

(37 citation statements)

References 71 publications

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“…[Bmim][NO 3 ]) 144. Therefore, further research concerning ammonium-based ILs and proteins need to be carried out to clear all the confusions and development of better protein protecting solvents.…”

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confidence: 99%

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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confidence: 99%

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

Jha

Venkatesu

2015

Phys. Chem. Chem. Phys.

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“…Kratky plots provide insight into the compactness of a protein, i.e., a bell shape in the plot indicates a globular protein, whereas a plateau, seen in the high q region, suggests that the protein is unfolded. Next, we measured the changes in the tertiary structure of both proteins induced by [bmim] [NO 3 ] using near-UV CD spectroscopy (Figure 3a and b [24][25][26][27][28]. Figure 4 summarizes the structural transitions of proteins in aqueous solutions over a wide IL concentration range.…”

Section: Structural Transition Of Proteins In Aqueous Solutions With mentioning

confidence: 99%

Ionic Liquid-Induced Unique Structural Transitions of Proteins

Takekiyo¹,

Yoshimura²

2017

Progress and Developments in Ionic Liquids

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The structural transitions of proteins in aqueous solutions of various ionic liquids (ILs) over a wide concentration range (x (mol% IL) = 0-30) were investigated using Fouriertransform infrared and near-UV circular dichroism spectroscopy combined with small-angle X-ray scattering. The proteins in the aqueous IL solutions showed two structural transition patterns: (i) the folded state → unfolded state → partial globular state (α-helical formation disrupted tertiary structure) and (ii) the folded state → unfolded state → aggregation (amyloid-like aggregation or disordered aggregation). We found that the helical formation of proteins in the condensed IL solutions was strongly related to the competition between the low polarity and denaturation effect of ions. Moreover, the amyloid-like aggregate formation correlated with the competition between the size of the confined water assemblies in the IL layer and the IL-amino acid residue interactions. On the basis of these results, we discussed the future applications of ILs, including their use as cryoprotectants for proteins and as agents for the suppression of amyloid formation.

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“…We selected two ILs with different influences on protein stability and classification within the Hofmeister series including 1‐butyl‐3‐methylimidazolium thiocyanate ([bmim][SCN]) and the ethylammonium nitrate (EAN). The former has a strong protein denaturation ability in the Hofmeister series, while the latter has a weak protein denaturation ability relative to [bmim][SCN] and has a helix forming ability for protein . In addition, to analyze the aggregation selectivity of A β 1‐11 in aqueous IL solutions, we used Fourier‐transform infrared (FTIR) spectroscopy.…”

Section: Introductionmentioning

confidence: 99%

Aggregation selectivity of amyloid β_1‐11 peptide in aqueous ionic liquid solutions

et al. 2019

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Understanding the aggregation selectivity of peptide fragments of full‐length proteins in aqueous solutions with ionic liquids (ILs) could facilitate the elucidation of the relationship between the IL‐protein interactions and structural behavior of intrinsically disordered proteins (IDPs) such as amyloid β protein following the addition of ILs. In the present study, we investigate structural changes in peptide fragment 1‐11 (Aβ1‐11) of amyloid β protein in aqueous solutions with two ILs including 1‐butyl‐3‐methylimidazolium thiocyanate ([bmim][SCN]) and ethylammonium nitrate (EAN) using optical spectroscopy. The addition of [bmim][SCN], which exhibits strong protein denaturant ability, induced the formation of an intermolecular β‐sheet structure (aggregation), while the addition of EAN, which has a weaker denaturant ability compared with [bmim][SCN], did not cause aggregation. Since the role of cations is related to the ability to mask the charged residues of Aβ1‐11, the aggregation selectivity of Aβ1‐11 depends on the anionic species and anions with high denaturation ability enhanced aggregation. Our results demonstrated that the structural change in peptide fragment in aqueous IL solutions could be used to evaluate the relationship between the IL‐protein interactions and aggregation selectivity in IDPs in aqueous IL solutions.

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Ionic Liquid-Induced Formation of the α-Helical Structure of β-Lactoglobulin

Cited by 43 publications

References 71 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

Ionic Liquid-Induced Unique Structural Transitions of Proteins

Aggregation selectivity of amyloid β_1‐11 peptide in aqueous ionic liquid solutions

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Ionic Liquid-Induced Formation of the α-Helical Structure of β-Lactoglobulin

Cited by 43 publications

References 71 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

Ionic Liquid-Induced Unique Structural Transitions of Proteins

Aggregation selectivity of amyloid β1‐11 peptide in aqueous ionic liquid solutions

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Aggregation selectivity of amyloid β_1‐11 peptide in aqueous ionic liquid solutions