Linking Trehalose Self-Association with Binary Aqueous Solution Equation of State

Sapir, Liel; Harries, Daniel

doi:10.1021/jp109780n

Cited by 66 publications

(109 citation statements)

References 86 publications

(199 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The most intense features in the dataset correspond to singly-and doubly-protonated tripeptide ions, ions, where n=3-7. The presence of these disaccharide clusters in these spectra is consistent with the relatively high disaccharide concentration (1.2 mM total saccharide concentration) and the known tendency of some of these molecules to self-associate in aqueous environments [38]. It is interesting to note that these clusters only incorporate a single tripeptide.…”

Section: Screening Peptide Reagents Against Disaccharidessupporting

confidence: 78%

Biologically-Inspired Peptide Reagents for Enhancing IMS-MS Analysis of Carbohydrates

Bohrer

Clemmer

2011

J. Am. Soc. Mass Spectrom.

View full text Add to dashboard Cite

The binding properties of a peptidoglycan recognition protein are translated via combinatorial chemistry into short peptides. Non-adjacent histidine, tyrosine, and arginine residues in the protein's binding cleft that associate specifically with the glycan moiety of a peptidoglycan substrate are incorporated into linear sequences creating a library of 27 candidate tripeptide reagents (three possible residues permutated across three positions). Upon electrospraying the peptide library and carbohydrate mixtures, some noncovalent complexes are observed. The binding efficiencies of the peptides vary according to their amino acid composition as well as the disaccharide linkage and carbohydrate ring-type. In addition to providing a charge-carrier for the carbohydrate, peptide reagents can also be used to differentiate carbohydrate isomers by ion mobility spectrometry. The utility of these peptide reagents as a means of enhancing ion mobility analysis of carbohydrates is illustrated by examining four glucose-containing disaccharide isomers, including a pair that is not resolved by ion mobility alone. The specificity and stoichiometry of the peptide-carbohydrate complexes are also investigated. Trihistidine demonstrates both suitable binding efficiency and successful resolution of disaccharides isomers, suggesting it may be a useful reagent in IMS analyses of carbohydrates.

show abstract

Section: Screening Peptide Reagents Against Disaccharidessupporting

confidence: 78%

Biologically-Inspired Peptide Reagents for Enhancing IMS-MS Analysis of Carbohydrates

Bohrer

Clemmer

2011

J. Am. Soc. Mass Spectrom.

View full text Add to dashboard Cite

show abstract

“…As reported by several studies, the presence of hydrophilic hydroxyl groups of trehalose helps to form hydrogen bonds with the like molecules and as a result of this formation an extended trehalose hydrogen bond network takes place. 78,79 Due to the formation of this extended sugar−sugar hydrogen bond network, the dynamical properties of the solution species are greatly affected. 80 As reported earlier, the concentrated aqueous trehalose solution has a very high glass transition temperature and forms a highly viscous glassy matrix to keep the biomolecules fixed.…”

Section: Resultsmentioning

confidence: 99%

Exploring the Counteracting Mechanism of Trehalose on Urea Conferred Protein Denaturation: A Molecular Dynamics Simulation Study

Paul

2015

J. Phys. Chem. B

View full text Add to dashboard Cite

To provide the underlying mechanism of the inhibiting effect of trehalose on the urea denatured protein, we perform classical molecular dynamics simulations of N-methylacetamide (NMA) in aqueous urea and/or trehalose solution. The site-site radial distribution functions and hydrogen bond properties indicate in binary urea solution the replacement of NMA-water hydrogen bonds by NMA-urea hydrogen bonds. On the other hand, in ternary urea and trehalose solution, trehalose does not replace the NMA-urea hydrogen bonds significantly; rather, it forms hydrogen bonds with the NMA molecule. The calculation of a preferential interaction parameter shows that, at the NMA surface, trehalose molecules are preferred and the preference for urea decreases slightly in ternary solution with respect to the binary solution. The exclusion of urea molecules in the ternary urea-NMA-trehalose system causes alleviation in van der Waals interaction energy between urea and NMA molecules. Our findings also reveal the following: (a) trehalose and urea induced second shell collapse of water structure, (b) a reduction in the mean trehalose cluster size in ternary solution, and (c) slowing down of translational motion of solution species in the presence of osmolytes. Implications of these results for the molecular explanations of the counteracting mechanism of trehalose on urea induced protein denaturation are discussed.

show abstract

“…19,32,[57][58][59][60][61] To furnish a better quantitative scenario, we define clusters as the assembly of molecules which are within 3.5 Å from each other. Time variation of the number View Article Online of clusters of trehalose along with its cluster size at different concentrations was plotted (Fig.…”

Section: Clustering Of Trehalosementioning

confidence: 99%

Revisiting the conundrum of trehalose stabilization

Katyal

Deep

2014

Phys. Chem. Chem. Phys.

View full text Add to dashboard Cite

Protein aggregation and loss of protein's biological functionality are manifestations of protein instability. Cosolvents, in particular trehalose, are widely accepted antidotes against such destabilization. Although numerous theories have been promulgated in the literature with regard to its mechanism of stabilization, the present scenario is still elusive in view of the discrepancies existing in them. To this end, we have revisited the conundrum and attempted to rationalize the mechanism by conducting thorough investigation of the effect of trehalose on the native, partially unfolded and denatured states of protein "Lysozyme" by means of molecular dynamic (MD) simulations under different temperature and concentration regimes. Two-dimensional contour plots along with principal component analysis suggest that trehalose molecules offer on-pathway stabilization unaltering the principal direction of protein's motion, although it slows down protein dynamics so that the protein gets trapped in the homogeneous ensemble of conformations closer to the native state. Free energy landscape reveals higher population of native compared to intermediate and denatured states. Delphi results and calculation of the preferential interaction parameter demonstrate that this relative stabilization of the native state can be ascribed to be the consequence of favourable interactions of trehalose with side chains of certain loci on the protein surface encompassing polar flexible residues. Stability of protein results from the observed difference in binding affinity of trehalose for native and denatured states of protein. Our findings are at variance with the common conception of relative destabilization of the denatured state. Rather, we provide evidence for relative stabilization of the native state. This stabilization is due to interplay of protein-trehalose, water-trehalose, water-water, protein-water and trehalose-trehalose interactions.

show abstract

Linking Trehalose Self-Association with Binary Aqueous Solution Equation of State

Cited by 66 publications

References 86 publications

Biologically-Inspired Peptide Reagents for Enhancing IMS-MS Analysis of Carbohydrates

Biologically-Inspired Peptide Reagents for Enhancing IMS-MS Analysis of Carbohydrates

Exploring the Counteracting Mechanism of Trehalose on Urea Conferred Protein Denaturation: A Molecular Dynamics Simulation Study

Revisiting the conundrum of trehalose stabilization

Contact Info

Product

Resources

About