RT Journal Article
T1 Hydration in Deep Eutectic Solvents Induces Non-monotonic Changes in the Conformation and Stability of Proteins
A1 Sánchez Fernández, Adrián
A1 Basic, Medina
A1 Xiang, Jenny
A1 Prevost, Sylvain
A1 Jackson, Andrew J.
A1 Dicko, Cedric
K1 Hydration
K1 Nucleic acid structure
K1 Peptides and proteins
K1 Protein structure
K1 Solvents
AB 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 % H2O) and high (>40 wt % H2O) 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 % H2O 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
PB ACS Publications
SN 0002-7863
YR 2022
FD 2022
LK http://hdl.handle.net/10347/29669
UL http://hdl.handle.net/10347/29669
LA eng
NO J. Am. Chem. Soc. 2022, 144, 51, 23657–23667
NO A.S.F. acknowledges the Spanish Ministerio de Universidades for the awarded Maria Zambrano fellowship. Also, the research in this study was performed with financial support from Vinnova─Swedish Governmental Agency for Innovation Systems within the NextBioForm Competence Centre and from The Crafoord Foundation (grant #20190750). The authors thank the Institute Laue-Langevin for the awarded beamtime (8-03-1049)
DS Minerva
RD 24 abr 2026