Structural adaptations in the bovine serum albumin protein in archetypal deep eutectic solvent reline and its aqueous mixtures

Kumari, Monika; Kumari, Pratibha; Kashyap, Hemant K.

doi:10.1039/d1cp05829k

Cited by 19 publications

(26 citation statements)

References 54 publications

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“…75 Here, it is observed that the change in the emission of the Trp residues of BSA in 1:2 ChCl:Glyc is opposite to that of the isolated amino acid. As most of these residues are buried in the hydrophobic core of the protein in the native state, 51,55,74 these changes cannot be solely attributed to solvent exposure and must relate to conformational transitions occurring in the protein, where the Trp side chains are relocated inside the protein envelope. In contrast, the bathochromic shifts observed at low hydration potentially relate to an increase in the solvent exposure of Trp and a more pronounced unfolding.…”

Section: ■ Resultsmentioning

confidence: 99%

Hydration in Deep Eutectic Solvents Induces Non-monotonic Changes in the Conformation and Stability of Proteins

et al. 2022

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The preservation of labile biomolecules presents a major challenge in chemistry, and deep eutectic solvents (DESs) have emerged as suitable environments for this purpose. However, how the hydration of DESs impacts the behavior of proteins is often neglected. Here, we demonstrate that the amino acid environment and secondary structure of two proteins (bovine serum albumin and lysozyme) and an antibody (immunoglobulin G) in 1:2 choline chloride:glycerol and 1:2 choline chloride:urea follow a re-entrant behavior with solvent hydration. A dome-shaped transition is observed with a folded or partially folded structure at very low (<10 wt % H 2 O) and high (>40 wt % H 2 O) DES hydration, while protein unfolding increases between those regimes. Hydration also affects protein conformation and stability, as demonstrated for bovine serum albumin in hydrated 1:2 choline chloride:glycerol. In the neat DES, bovine serum albumin remains partially folded and unexpectedly undergoes unfolding and oligomerization at low water content. At intermediate hydration, the protein begins to refold and gradually retrieves the native monomer−dimer equilibrium. However, ca. 36 wt % H 2 O is required to recover the native folding fully. The half-denaturation temperature of the protein increases with decreasing hydration, but even the dilute DESs significantly enhance the thermal stability of bovine serum albumin. Also, protein unfolding can be reversed by rehydrating the sample to the high hydration regime, also recovering protein function. This correlation provides a new perspective to understanding protein behavior in hydrated DESs, where quantifying the DES hydration becomes imperative to identifying the folding and stability of proteins.

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Section: ■ Resultsmentioning

confidence: 99%

Hydration in Deep Eutectic Solvents Induces Non-monotonic Changes in the Conformation and Stability of Proteins

et al. 2022

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“…This result is similar to the findings by Kumari et al , who observed that choline chloride–urea could form H bonds with BSA and affect its secondary structure; however, the protein backbone was preserved. 71…”

Section: Resultsmentioning

confidence: 99%

An innovative, low-cost and environment-friendly approach by using a deep eutectic solvent as the water substitute to minimize waste in the textile industry and for better clothing performance

et al. 2022

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“…Rigidity in the protein structure is also noted in the presence of pure reline. The authors concluded that, despite the expansion, the tertiary structure of BSA in pure reline was similar to the native protein structure [59].…”

Section: Stability Of Proteins In Deep Eutectic Solventsmentioning

confidence: 99%

“…More recently, the effect of pure and hydrated reline choline chloride/urea DES in the structural stability of BSA using all-atom molecular dynamics simulations was investigated by Kumari et al [59]. A considerable change in the BSA structure and an increment in the accessible surface area of the solvent were found.…”

Section: Stability Of Proteins In Deep Eutectic Solventsmentioning

confidence: 99%

An Overview on the Recent Advances in Alternative Solvents as Stabilizers of Proteins and Enzymes

et al. 2022

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Currently, the use of alternative solvents is increasing, namely ionic liquids (ILs) and deep eutectic solvents (DESs) in diverse fields of knowledge, such as biochemistry, chemistry, chemical engineering, biotechnology and biomedicine. Particularly, when compared to traditional solvents, these alternative solvents have great importance for biomolecules due to the enhanced solubility, structure stability and the biological activity of biomolecules, such as protein and enzymes. Thus, in this review article, the recent developments and efforts on the technological developments carried out with ILs and DESs for the stabilization and activation of proteins and enzymes are provided. The most studied IL- and DES-based formulations for proteins and enzymes are discussed and the molecular mechanisms and interactions related to the increased stability promoted by these alternative solvents are disclosed, while emphasizing their main advantages.

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Structural adaptations in the bovine serum albumin protein in archetypal deep eutectic solvent reline and its aqueous mixtures

Abstract: The global concern over the environmental impact and challenges associated with the use of conventional solvents in bio-transformation processes have pushed the search for alternative solvents. Recently, deep eutectic solvents...

Cited by 19 publications

References 54 publications

Hydration in Deep Eutectic Solvents Induces Non-monotonic Changes in the Conformation and Stability of Proteins

Hydration in Deep Eutectic Solvents Induces Non-monotonic Changes in the Conformation and Stability of Proteins

An innovative, low-cost and environment-friendly approach by using a deep eutectic solvent as the water substitute to minimize waste in the textile industry and for better clothing performance

An Overview on the Recent Advances in Alternative Solvents as Stabilizers of Proteins and Enzymes

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