Comparative study of trehalose, sucrose and maltose in water solutions by molecular modelling

Bordat, Patrice; Lerbret, Adrien; Demaret, J.; Affouard, Frédéric; Descamps, M.

doi:10.1209/epl/i2003-10052-0

Cited by 119 publications

(128 citation statements)

References 24 publications

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“…The second band near 170-200 cm -1 has been previously assigned to collective intermolecular O-H ... O stretching vibrations [37]. The decrease of its amplitude when the sugar concentration increases reflects the destructuring effect of sugars on the HBN of water [9,19,28,38], which essentially stem from the numerous HBs they form with water [27].…”

Section: Low-frequency Vibrational Dynamicsmentioning

confidence: 97%

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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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Section: Low-frequency Vibrational Dynamicsmentioning

confidence: 97%

“…In particular, the sugar-induced blue shift of the second band implies that water-water HBs are strengthened, as will be shown more explicitely in section 3.3. properties of disaccharide/water solutions [27,28]. Fig.…”

Section: Low-frequency Vibrational 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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“…For example, studies that concentrate on the physical or chemical properties of trehalose and its solution pay little attention to finding out a correlation with biological activity. [3][4][5][6][7][8][9][10][11] Similarly, articles reporting gene expression profiling relevant to trehalose as a bioprotector do not make a serious attempt to relate the protective action to physical and chemical properties of the molecule. [12][13][14][15][16][17] This review attempts to bridge this gap and to find out how data from physicists, chemists, and life scientists can be collected and collated so that an understanding of general interest to protein scientists may emerge.…”

Section: Introductionmentioning

confidence: 99%

Effect of trehalose on protein structure

Jain¹,

Roy²

2008

Protein Science

733

576

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Trehalose is a ubiquitous molecule that occurs in lower and higher life forms but not in mammals. Till about 40 years ago, trehalose was visualized as a storage molecule, aiding the release of glucose for carrying out cellular functions. This perception has now changed dramatically. The role of trehalose has expanded, and this molecule has now been implicated in a variety of situations. Trehalose is synthesized as a stress-responsive factor when cells are exposed to environmental stresses like heat, cold, oxidation, desiccation, and so forth. When unicellular organisms are exposed to stress, they adapt by synthesizing huge amounts of trehalose, which helps them in retaining cellular integrity. This is thought to occur by prevention of denaturation of proteins by trehalose, which would otherwise degrade under stress. This explanation may be rational, since recently, trehalose has been shown to slow down the rate of polyglutamine-mediated protein aggregation and the resultant pathogenesis by stabilizing an aggregation-prone model protein. In recent years, trehalose has also proved useful in the cryopreservation of sperm and stem cells and in the development of a highly reliable organ preservation solution. This review aims to highlight the changing perception of the role of trehalose over the last 10 years and to propose common mechanisms that may be involved in all the myriad ways in which trehalose stabilizes protein structures. These will take into account the structure of trehalose molecule and its interactions with its environment, and the explanations will focus on the role of trehalose in preventing protein denaturation.

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“…This arrangement gives the molecule an unusual flexibility around the disaccharide bond, which may allow it to fit more closely with the irregular surface of macromolecules than other, more rigid disaccharides, in which the rings are directly hydrogen bonded to each other (Colac¸o & Roser, 1995). According to Bordat, Lerbret, Demaret, Affouard, and Descamps (2004) trehalose has superior effects in ''destructuring'' the network of water and in slowing down its dynamics. This property could play a key role in the understanding of the microscopic mechanisms of bioprotection.…”

Section: Resultsmentioning

confidence: 99%