Homotactic and heterotactic interactions in aqueous solutions containing some saccharides. Experimental results and an empirical relationship between saccharide solvation and solute–solute interactions

Gaffney, Simon H.; Haslam, Edwin; Lilley, Terence H.; Ward, Tracy R.

doi:10.1039/f19888402545

Cited by 29 publications

(11 citation statements)

References 1 publication

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“…However, in sucrose, intramolecular HBs are present (57) thus leaving an overall lower number of sites available to HB with the surrounding. At variance, in agreement with the large number of coordination water molecules present in its (pentahydrate) crystalline state (58), raffinose directly binds a larger fraction of water molecules than the other sugars (59), as confirmed also by the r A value for sample 2 R .…”

Section: Water-protein-sugar Interactionssupporting

confidence: 63%

Role of Solvent on Protein-Matrix Coupling in MbCO Embedded in Water-Saccharide Systems: A Fourier Transform Infrared Spectroscopy Study

Giuffrida

Cottone

Cordone

2006

Biophysical Journal

130

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Embedding protein in sugar systems of low water content enables one to investigate the protein dynamic-structure function in matrixes whose rigidity is modulated by varying the content of residual water. Accordingly, studying the dynamics and structure thermal evolution of a protein in sugar systems of different hydration constitutes a tool for disentangling solvent rigidity from temperature effects. Furthermore, studies performed using different sugars may give information on how the detailed composition of the surrounding solvent affects the internal protein dynamics and structural evolution. In this work, we compare Fourier transform infrared spectroscopy measurements (300-20 K) on MbCO embedded in trehalose, sucrose, maltose, raffinose, and glucose matrixes of different water content. At all the water contents investigated, the protein-solvent coupling was tighter in trehalose than in the other sugars, thus suggesting a molecular basis for the trehalose peculiarity. These results are in line with the observation that protein-matrix phase separation takes place in lysozyme-lactose, whereas it is absent in lysozyme-trehalose systems; indeed, these behaviors may respectively be due to the lack or presence of suitable water-mediated hydrogen-bond networks, which match the protein surface to the surroundings. The above processes might be at the basis of pattern recognition in crowded living systems; indeed, hydration shells structural and dynamic matching is first needed for successful come together of interacting biomolecules.

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Section: Water-protein-sugar Interactionssupporting

confidence: 63%

Role of Solvent on Protein-Matrix Coupling in MbCO Embedded in Water-Saccharide Systems: A Fourier Transform Infrared Spectroscopy Study

Giuffrida

Cottone

Cordone

2006

Biophysical Journal

130

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“…The efficiency of trehalose may be due to its ability in forming glassy structures in a wide hydration range, along with the hydrogen bond capability. However, this is not consistent with results on raffinose, which is less effective than other sugars [9], although it has a glass transition temperature comparable with that of trehalose, along with larger hydrogen bonding potential [10]. An approach based on structural studies of trehalosewater binary systems, proposes that the polymorphism of trehalose both in the crystalline and amorphous states is at the basis of its effectiveness [11].…”

Section: Introductioncontrasting

confidence: 41%

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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“…Actually, trehalose was found more effective than other disaccharides at high temperatures, when direct interactions between the sugar and the biomolecule should play a stronger role. However, this model cannot explain results on raffinose [27]: this sugar is less-effective, despite having a Tg similar to trehalose, and an even larger hydrogen bonding capability [28]. It has also been shown that glass formation alone does not provide the best suppression of protein motions: either liquid or glassy glycerol provides stronger effects than glassy trehalose at low temperature, while trehalose appears most effective at high temperatures [29].…”

Section: The Trehalose Peculiaritymentioning

confidence: 73%

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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Homotactic and heterotactic interactions in aqueous solutions containing some saccharides. Experimental results and an empirical relationship between saccharide solvation and solute–solute interactions

Cited by 29 publications

References 1 publication

Role of Solvent on Protein-Matrix Coupling in MbCO Embedded in Water-Saccharide Systems: A Fourier Transform Infrared Spectroscopy Study

Role of Solvent on Protein-Matrix Coupling in MbCO Embedded in Water-Saccharide Systems: A Fourier Transform Infrared Spectroscopy Study

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

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

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