Impact of imidazolium-based ionic liquids on the structure and stability of lysozyme

Satish, Lakkoji; Rana, Shubhasmin; Arakha, Manoranjan; Rout, Lipeeka; Ekka, Basanti; Jha, Suman; Dash, Priyabrat; Sahoo, Harekrushna

doi:10.1080/00387010.2016.1167089

Cited by 42 publications

(29 citation statements)

References 56 publications

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“…A specific family has grown in this direction, the surface-active ionic liquids (SAILs), which are characterized by their enhanced solubilization mechanisms due to their amphiphilic nature granted by the long cationic and/or anionic hydrogenated chains. The superior surface activity of SAILs compared with conventional surfactants allows self-assembly in aqueous solutions into more efficient colloidal systems, such as micelles or vesicles, with greater control of their shape, size, stability, and specific utility [7,[10][11][12][13][14][15][16]. These advantages highlight the substitution of surfactants by SAILs in the protein stability field, successfully demonstrated by some works in the specific case of lysozyme.…”

Section: Introductionmentioning

confidence: 99%

Unveiling the Influence of Non-Toxic Fluorinated Ionic Liquids Aqueous Solutions in the Encapsulation and Stability of Lysozyme

Ferreira

Vieira

Araújo

et al. 2021

Sustainable Chemistry

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Proteins are bioactive compounds with high potential to be applied in the biopharmaceutical industry, food science and as biocatalysts. However, protein stability is very difficult to maintain outside of the native environment, which hinders their applications. Fluorinated ionic liquids (FILs) are a promising family of surface-active ionic liquids (SAILs) that have an amphiphilic behavior and the ability to self-aggregate in aqueous solutions by the formation of colloidal systems. In this work, the protein lysozyme was selected to infer on the influence of FILs in its stability and activity. Then, the cytotoxicity of FILs was determined to evaluate their biocompatibility, concluding that the selected compounds have neglected cytotoxicity. Therefore, UV–visible spectroscopy was used to infer the FIL-lysozyme interactions, concluding that the predominant interaction is the encapsulation of the lysozyme by FILs. The encapsulation efficiency was also tested, which highly depends on the concentration and anion of FIL. Finally, the bioactivity and thermal stability of lysozyme were evaluated, and the encapsulated lysozyme keeps its activity and thermal stability, concluding that FILs can be a potential stabilizer to be used in protein-based delivery systems.

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Section: Introductionmentioning

confidence: 99%

Unveiling the Influence of Non-Toxic Fluorinated Ionic Liquids Aqueous Solutions in the Encapsulation and Stability of Lysozyme

Ferreira

Vieira

Araújo

et al. 2021

Sustainable Chemistry

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“…In most of these earlier studies, the IL concentration was limited to the millimolar range (< 10 mM). Previous work by our group revealed that the concentration of ILs (0.2–1.0 M) has a stabilizing effect on protein stability . Therefore, in this work, we focused on the effect on protein structure and stability exerted by the type of ILs as well as their concentration (0.2–1.0 M).…”

Section: Introductionmentioning

confidence: 99%

Spectroscopic insight into the interaction of bovine serum albumin with imidazolium‐based ionic liquids in aqueous solution

2016

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The study of protein–ionic liquid interactions is very important because of the widespread use of ionic liquids as protein stabilizer in the recent years. In this work, the interaction of bovine serum albumin (BSA) with different imidazolium‐based ionic liquids (ILs) such as [1‐ethyl‐3‐methyl‐imidazolium ethyl sulfate (EmimESO4), 1‐ethyl‐3‐methyl‐imidazolium chloride (EmimCl) and 1‐butyl‐3‐methyl‐imidazolium chloride (BmimCl)] has been investigated using different spectroscopic techniques. The intrinsic fluorescence of BSA is quenched by ILs by the dynamic mechanism. The thermodynamic analysis demonstrates that very weak interactions exist between BSA and ILs. 8‐Anilino‐1‐naphthalenesulfonic acid (ANS) fluorescence and lifetime measurements reveal the formation of the compact structure of BSA in IL medium. The conformational changes of BSA were monitored by CD analysis. Temperature‐dependent ultraviolet (UV) measurements were done to study the thermal stability of BSA. The thermal stability of BSA in the presence of ILs follows the trend EmimESO4 > EmimCl > BmimCl and in the presence of more hydrophobic IL, destabilization increases rapidly as a function of concentration.

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“…70 Furthermore, the positive values of ΔH (4.35 KJ•mol −1 ) and TΔS (0.03 KJ•mol −1 •K −1 ) clearly indicate that the binding is entropically driven. 71 According to Ross's thermodynamic laws for the binding between small molecules and biomacromolecules, this type of entropic control of the binding process indicates that the hydrophobic interactions may play a predominant role in HSA-AntiOxCIN 3 association. 70 Gathering all the outcomes provided by fluorescence methods it was possible to predict a hydrophobic interaction between AntiOxCIN 3 and the Tyr residue of HSA with a consequent protein conformational change that promotes the exposure of Trp residues to aqueous solution.…”

Section: Results and Discussion Interaction Studies With Micelles Modmentioning

confidence: 99%

Lipid Nanosystems and Serum Protein as Biomimetic Interfaces: Predicting the Biodistribution of a Caffeic Acid-Based Antioxidant

Fernandes

Benfeito

Cagide

et al. 2021

NSA

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AntiOxCIN 3 is a novel mitochondriotropic antioxidant developed to minimize the effects of oxidative stress on neurodegenerative diseases. Prior to an investment in preclinical in vivo studies, it is important to apply in silico and biophysical cell-free in vitro studies to predict AntiOxCIN 3 biodistribution profile, respecting the need to preserve animal health in accordance with the EU principles (Directive 2010/63/EU). Accordingly, we propose an innovative toolbox of biophysical studies and mimetic models of biological interfaces, such as nanosystems with different compositions mimicking distinct membrane barriers and human serum albumin (HSA). Methods: Intestinal and cell membrane permeation of AntiOxCIN 3 was predicted using derivative spectrophotometry. AntiOxCIN 3-HSA binding was evaluated by intrinsic fluorescence quenching, synchronous fluorescence, and dynamic/electrophoretic light scattering. Steady-state and time-resolved fluorescence quenching was used to predict AntiOxCIN 3membrane orientation. Fluorescence anisotropy, synchrotron small-and wide-angle X-ray scattering were used to predict lipid membrane biophysical impairment caused by AntiOxCIN 3 distribution. Results and Discussion: We found that AntiOxCIN 3 has the potential to permeate the gastrointestinal tract. However, its biodistribution and elimination from the body might be affected by its affinity to HSA (>90%) and by its steady-state volume of distribution (VD SS =1.89 ± 0.48 L•Kg −1). AntiOxCIN 3 is expected to locate parallel to the membrane phospholipids, causing a bilayer stiffness effect. AntiOxCIN 3 is also predicted to permeate through blood-brain barrier and reach its therapeutic target-the brain. Conclusion: Drug interactions with biological interfaces may be evaluated using membrane model systems and serum proteins. This knowledge is important for the characterization of drug partitioning, positioning and orientation of drugs in membranes, their effect on membrane biophysical properties and the study of serum protein binding. The analysis of these interactions makes it possible to collect valuable knowledge on the transport, distribution, accumulation and, eventually, therapeutic impact of drugs which may aid the drug development process.

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Impact of imidazolium-based ionic liquids on the structure and stability of lysozyme

Cited by 42 publications

References 56 publications

Unveiling the Influence of Non-Toxic Fluorinated Ionic Liquids Aqueous Solutions in the Encapsulation and Stability of Lysozyme

Unveiling the Influence of Non-Toxic Fluorinated Ionic Liquids Aqueous Solutions in the Encapsulation and Stability of Lysozyme

Spectroscopic insight into the interaction of bovine serum albumin with imidazolium‐based ionic liquids in aqueous solution

Lipid Nanosystems and Serum Protein as Biomimetic Interfaces: Predicting the Biodistribution of a Caffeic Acid-Based Antioxidant

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