Light Scattering Spectra of Water in Trehalose Aqueous Solutions: Evidence for Two Different Solvent Relaxation Processes

Paolantoni, Marco; Comez, Lucia; Gallina, Maria Elena; Sassi, Paola; Scarponi, F.; Fioretto, D.; Morresi, Assunta

doi:10.1021/jp9004983

Cited by 56 publications

(98 citation statements)

References 33 publications

(105 reference statements)

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“…Solvent collective motions could set up, depending on the solute; if solute molecules are not involved in hydrogen bonding, such long-range coherence reduces or even fails. In this respect, light scattering measurements on trehalose-water solutions in a wide frequency range (GHz to THz) [159] reveal two separate solvent relaxation processes: a slow one, related to the solute dynamics, ascribed to hydration water, and a fast one ascribed to bulk solvent. These results were confirmed by MD simulations [160] and in presence of protein [161].…”

Section: T F O R D I S T R I B U T I O Nmentioning

confidence: 99%

Proteins in Saccharides Matrices and the Trehalose Peculiarity: Biochemical and Biophysical Properties

Cordone¹,

Cupane²,

Emanuele

et al. 2015

COC

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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.

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Section: T F O R D I S T R I B U T I O Nmentioning

confidence: 99%

Proteins in Saccharides Matrices and the Trehalose Peculiarity: Biochemical and Biophysical Properties

Cordone¹,

Cupane²,

Emanuele

et al. 2015

COC

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“…3), the water-water HBs activation energy is found the highest in the trehalose solution at 66 wt %, even though the related large error bars prevent any statistically meaningful comparison between the three sugars. showed a strong retardation of the dynamics of water molecules hydrating sugars [15,20,21,22], up to distances of 5.5-6.5 Å for disaccharides (trehalose, sucrose, lactose), that is, beyond their first static solvation layer. In particular, water-water HB lifetimes were found to increase by as much as 40 % compared to the bulk in the vicinity of trehalose and lactose [15,21], because sugar-water HBs are more stable than water-water HBs [20].…”

Section: Water Hydrogen Bonds Dynamicsmentioning

confidence: 99%

Slowing down of water dynamics in disaccharide aqueous solutions

Lerbret¹,

Affouard²,

Bordat³

et al. 2011

Journal of Non-Crystalline Solids

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The dynamics of water in aqueous solutions of three homologous disaccharides, namely trehalose, maltose and sucrose, has been analyzed by means of molecular dynamics simulations in the 0-66 wt % concentration range. The low-frequency vibrational densities of states (VDOS) of water were compared with the susceptibilities chi" of 0-40 wt % solutions of trehalose in D2O obtained from complementary Raman scattering experiments. Both reveal that sugars significantly stiffen the local environments experienced by water. Accordingly, its translational diffusion coefficient decreases when the sugar concentration increases, as a result of an increase of water-water hydrogen bonds lifetimes and of the corresponding activation energies. This induced slowing down of water dynamics, ascribed to the numerous hydrogen bonds that sugars form with water, is strongly amplified at concentrations above 40 wt % by the percolation of the hydrogen bond network of sugars, and may partially explain their well-known stabilizing effect on proteins in aqueous solutions.Comment: 14 pages, 4 figures, accepted in Journal of Non-Crystalline Solids (proceedings of the conference IDMRCS6

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“…In this respect, light scattering spectra on aqueous solutions of trehalose, recorded in a very wide frequency range (0.6-36000 GHz) [37], indicate the presence of two separate solvent relaxation processes: a slow one, related to the solute dynamics, ascribed to hydrating water, and a fast one ascribed to bulk solvent. These results were confirmed by MD simulations [38] and in presence of protein [39].…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2013

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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.

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Light Scattering Spectra of Water in Trehalose Aqueous Solutions: Evidence for Two Different Solvent Relaxation Processes

Cited by 56 publications

References 33 publications

Proteins in Saccharides Matrices and the Trehalose Peculiarity: Biochemical and Biophysical Properties

Proteins in Saccharides Matrices and the Trehalose Peculiarity: Biochemical and Biophysical Properties

Slowing down of water dynamics in disaccharide aqueous solutions

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

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