Title:Proteins in Saccharides Matrices and the Trehalose Peculiarity: Biochemical and Biophysical Properties
VOLUME: 19 ISSUE: 17
Author(s):Lorenzo Cordone, Grazia Cottone, Antonio Cupane, Antonio Emanuele, Sergio Giuffrida and Matteo Levantino
Affiliation:Department of Physics and Chemistry, University of Palermo, Italy.
Keywords:Biopreservation, glasses, myoglobin, protein dynamics, trehalose.
Abstract:Immobilization of proteins and other biomolecules in saccharide matrices leads to a series of peculiar
properties that are relevant from the point of view of both biochemistry and biophysics, and have important implications
on related fields such as food industry, pharmaceutics, and medicine. In the last years, the properties of
biomolecules embedded into glassy matrices and/or highly concentrated solutions of saccharides have been thoroughly
investigated, at the molecular level, through in vivo, in vitro, and in silico studies. These systems show an
outstanding ability to protect biostructures against stress conditions; various mechanisms appear to be at the basis
of such bioprotection, that in the case of some sugars (in particular trehalose) is peculiarly effective.
Here we review recent results obtained in our and other laboratories on ternary protein- sugar-water systems that have been typically
studied in wide ranges of water content and temperature. Data from a large set of complementary experimental techniques provide a consistent
description of structural, dynamical and functional properties of these systems, from atomistic to thermodynamic level.
In the emerging picture, the stabilizing effect induced on the encapsulated systems might be attributed to a strong biomolecule-matrix
coupling, mediated by extended hydrogen-bond networks, whose specific properties are determined by the saccharide composition and
structure, and depend on water content.
