How do trehalose, maltose and sucrose influence some structural and dynamical properties of lysozyme ? An insight from Molecular Dynamics simulations

TL;DR

This study uses molecular dynamics simulations to examine how trehalose, maltose, and sucrose affect the structural stability and dynamics of lysozyme, revealing that sugars mainly influence protein relaxation times through hydrogen-bond network percolation.

Contribution

It provides new insights into how disaccharides modulate protein dynamics and hydration, highlighting the role of hydrogen-bond network percolation in these effects.

Findings

Sugars weakly affect lysozyme conformation.

Sugars significantly increase protein relaxation times.

Hydrogen-bond network percolation correlates with dynamical changes.

Abstract

The influence of three well-known disaccharides, namely trehalose, maltose and sucrose, on some structural and dynamical properties of lysozyme has been investigated by means of molecular dynamics computer simulations in the 37-60 wt % concentration range. The effects of sugars on the protein conformation are found relatively weak, in agreement with the preferential hydration of lysozyme. Conversely, sugars seem to increase significantly the relaxation times of the protein. These effects are shown to be correlated to the fractional solvent accessibilities of lysozyme residues and further support the slaving of protein dynamics. Moreover, a significant increase in the relaxation times of lysozyme, sugars and water molecules is observed within the studied concentration range and may result from the percolation of the hydrogen-bond network of sugar molecules. This percolation appears to be of primary importance to explain the influence of sugars on the dynamical properties of lysozyme and water.