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Updated: Jun 5, 2026

Rapid One-step Enzymatic Synthesis and All-aqueous Purification of Trehalose Analogues

Rapid One-step Enzymatic Synthesis and All-aqueous Purification of Trehalose Analogues

Published on: February 17, 2017

Linking trehalose self-association with binary aqueous solution equation of state.

Liel Sapir¹, Daniel Harries

¹Institute of Chemistry and The Fritz Haber Research Center, The Hebrew University of Jerusalem, Safra Campus, Jerusalem 91904, Israel.

The Journal of Physical Chemistry. B

|December 29, 2010

Summary

Trehalose forms clusters in water, impacting its protective role. Simulations and experiments explored trehalose association, revealing insights into its solution behavior and interactions.

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Area of Science:

Biophysical chemistry
Solution thermodynamics
Computational biophysics

Background:

Trehalose is a disaccharide known for its protective properties.
Hydrogen bonding influences trehalose's interaction with water and self-association.
Concentration-dependent aggregation of trehalose may affect its function as a cosolute.

Purpose of the Study:

To investigate trehalose association in aqueous solutions across a wide concentration range.
To compare molecular dynamics simulations with experimental vapor pressure osmometry data.
To understand the interplay of repulsive and attractive forces in trehalose solutions.

Main Methods:

Molecular dynamics simulations using two distinct force fields.
Vapor pressure osmometry to measure osmotic pressure.
Analysis of trehalose cluster size and fractal dimension in simulations.

Main Results:

Estimated trehalose cluster percolation threshold between 1.5-2.2 m using simulations.
Experimental trehalose solutions exhibited positive deviations from ideal van't Hoff's law.
Simulations reasonably represented the solution equation of state but showed slight negative deviations.

Conclusions:

Trehalose aggregation is a key factor in its solution behavior.
Discrepancies between simulations and experiments suggest force field overestimation of trehalose aggregation.
Further refinement of force fields is needed for accurate modeling of trehalose-trehalose interactions.