Eur. Phys. J. E (2013) 36: 79
https://doi.org/10.1140/epje/i2013-13079-x

Regular Article

Proteins in amorphous saccharide matrices: Structural and dynamical insights on bioprotection

¹⁹⁸⁹⁴ Dipartimento di Fisica e Chimica, Università degli Studi di Palermo, Via Archirafi 36, I-90123, Palermo, Italy
²⁹⁸⁹⁴ Unité Materiaux et Transformations UMR CNRS 8207, Université Lille 1, UFR de Physique Bât P5, 59655, Villeneuve d’Ascq, France

^* e-mail: giuffrid@fisica.unipa.it

Received: 15 November 2012
Revised: 21 March 2013
Accepted: 2 May 2013
Published online: 17 July 2013

Abstract

Bioprotection by sugars, and in particular trehalose peculiarity, is a relevant topic due to the implications in several fields. The underlying mechanisms are not yet clearly elucidated, and remain the focus of current investigations. Here we revisit data obtained at our lab on binary sugar/water and ternary protein/sugar/water systems, in wide ranges of water content and temperature, in the light of the current literature. The data here discussed come from complementary techniques (Infrared Spectroscopy, Molecular Dynamics simulations, Small Angle X-ray Scattering and Calorimetry), which provided a consistent description of the bioprotection by sugars from the atomistic to the macroscopic level. We present a picture, which suggests that protein bioprotection can be explained in terms of a strong coupling of the biomolecule surface to the matrix via extended hydrogen-bond networks, whose properties are defined by all components of the systems, and are strongly dependent on water content. Furthermore, the data show how carbohydrates having similar hydrogen-bonding capabilities exhibit different efficiency in preserving biostructures.