Stabilization of Non-Native Folds and Programmable Protein Gelation in Compositionally Designed Deep Eutectic Solvents
Sanchez-Fernandez, Adrian ; Poon, Jia Fei ; Leung, Anna Elizabeth ; Prévost, Sylvain François and Dicko, Cedric LU
(2024)
In ACS Nano
18(28).
p.18314-18326
- Abstract
Proteins are adjustable units from which biomaterials with designed properties can be developed. However, non-native folded states with controlled topologies are hardly accessible in aqueous environments, limiting their prospects as building blocks. Here, we demonstrate the ability of a series of anhydrous deep eutectic solvents (DESs) to precisely control the conformational landscape of proteins. We reveal that systematic variations in the chemical composition of binary and ternary DESs dictate the stabilization of a wide range of conformations, that is, compact globular folds, intermediate folding states, or unfolded chains, as well as controlling their collective behavior. Besides, different conformational states can be visited by... (More)
Proteins are adjustable units from which biomaterials with designed properties can be developed. However, non-native folded states with controlled topologies are hardly accessible in aqueous environments, limiting their prospects as building blocks. Here, we demonstrate the ability of a series of anhydrous deep eutectic solvents (DESs) to precisely control the conformational landscape of proteins. We reveal that systematic variations in the chemical composition of binary and ternary DESs dictate the stabilization of a wide range of conformations, that is, compact globular folds, intermediate folding states, or unfolded chains, as well as controlling their collective behavior. Besides, different conformational states can be visited by simply adjusting the composition of ternary DESs, allowing for the refolding of unfolded states and vice versa. Notably, we show that these intermediates can trigger the formation of supramolecular gels, also known as eutectogels, where their mechanical properties correlate to the folding state of the protein. Given the inherent vulnerability of proteins outside the native fold in aqueous environments, our findings highlight DESs as tailorable solvents capable of stabilizing various non-native conformations on demand through solvent design.
(Less)
- author
- Sanchez-Fernandez, Adrian
; Poon, Jia Fei
; Leung, Anna Elizabeth
; Prévost, Sylvain François
and Dicko, Cedric
LU
- organization
- publishing date
- 2024-07
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- deep eutectic solvent, folding intermediates, protein conformation, protein eutectogel, supramolecular entanglement
- in
- ACS Nano
- volume
- 18
- issue
- 28
- pages
- 13 pages
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- scopus:85197311853
- pmid:38949563
- ISSN
- 1936-0851
- DOI
- 10.1021/acsnano.4c01950
- language
- English
- LU publication?
- yes
- id
- 153e9172-797e-4458-84ec-eebc0e86caf9
- date added to LUP
- 2024-09-23 12:36:01
- date last changed
- 2024-09-23 12:36:57
@article{153e9172-797e-4458-84ec-eebc0e86caf9,
abstract = {{<p>Proteins are adjustable units from which biomaterials with designed properties can be developed. However, non-native folded states with controlled topologies are hardly accessible in aqueous environments, limiting their prospects as building blocks. Here, we demonstrate the ability of a series of anhydrous deep eutectic solvents (DESs) to precisely control the conformational landscape of proteins. We reveal that systematic variations in the chemical composition of binary and ternary DESs dictate the stabilization of a wide range of conformations, that is, compact globular folds, intermediate folding states, or unfolded chains, as well as controlling their collective behavior. Besides, different conformational states can be visited by simply adjusting the composition of ternary DESs, allowing for the refolding of unfolded states and vice versa. Notably, we show that these intermediates can trigger the formation of supramolecular gels, also known as eutectogels, where their mechanical properties correlate to the folding state of the protein. Given the inherent vulnerability of proteins outside the native fold in aqueous environments, our findings highlight DESs as tailorable solvents capable of stabilizing various non-native conformations on demand through solvent design.</p>}},
author = {{Sanchez-Fernandez, Adrian and Poon, Jia Fei and Leung, Anna Elizabeth and Prévost, Sylvain François and Dicko, Cedric}},
issn = {{1936-0851}},
keywords = {{deep eutectic solvent; folding intermediates; protein conformation; protein eutectogel; supramolecular entanglement}},
language = {{eng}},
number = {{28}},
pages = {{18314--18326}},
publisher = {{The American Chemical Society (ACS)}},
series = {{ACS Nano}},
title = {{Stabilization of Non-Native Folds and Programmable Protein Gelation in Compositionally Designed Deep Eutectic Solvents}},
url = {{http://dx.doi.org/10.1021/acsnano.4c01950}},
doi = {{10.1021/acsnano.4c01950}},
volume = {{18}},
year = {{2024}},
}