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Rapid One-step Enzymatic Synthesis and All-aqueous Purification of Trehalose Analogues
Published on: February 17, 2017
Hydration and mobility of trehalose in aqueous solution
Louise Revsbech Winther1, Johan Qvist, Bertil Halle
1Department of Biophysical Chemistry, Center for Molecular Protein Science, Lund University, SE-22100 Lund, Sweden.
The Journal of Physical Chemistry. B
|July 20, 2012
Summary
Trehalose stabilizes proteins by altering water structure and dynamics. This study reveals direct trehalose-trehalose interactions and a modest impact on water
Area of Science:
- Biophysics
- Physical Chemistry
- Structural Biology
Background:
- Trehalose is a disaccharide known for stabilizing proteins against denaturation.
- The precise mechanism by which trehalose exerts its stabilizing effect, particularly concerning solvent interactions, remains unclear.
- Preferential exclusion of trehalose from protein surfaces suggests its influence on protein stability may be mediated by solvent modifications.
Purpose of the Study:
- To investigate how trehalose affects the structure and dynamics of water molecules in solution.
- To elucidate the role of solute-solute and solute-solvent interactions in trehalose's protein-stabilizing mechanism.
- To examine the rotational dynamics of trehalose and water across varying concentrations and temperatures.
Main Methods:
- Nuclear magnetic resonance (NMR) spectroscopy utilizing spin relaxation rates.
- Deuterated trehalose and (17)O-enriched water were used as probes.
- Measurements were conducted over a concentration range of 0.025-1.5 M and temperatures from 236 K to 293 K.
Main Results:
- Direct trehalose-trehalose interactions were observed, suggesting the formation of transient trehalose clusters.
- Trehalose exhibited a modest perturbation of water molecule rotation and hydrogen-bond exchange within the first hydration layer (a factor of 1.6 at 298 K).
- The deviation of trehalose's rotational dynamics from the Stokes-Einstein-Debye relation was explained by a dynamic solvent effect, better described by a local viscosity model accounting for bound water.
Conclusions:
- Trehalose influences protein stability through modifications in water structure and dynamics, including solute-solute clustering.
- A local viscosity model provides a more accurate description of the dynamic solvent effects associated with trehalose solutions.
- Understanding these solvent dynamics is crucial for fully explaining trehalose's protein-stabilizing properties.
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