The impact of kosmotropes and chaotropes on bulk and hydration shell water dynamics in a model peptide solution

Russo, Daniela

doi:10.1016/j.chemphys.2007.08.001

Cited by 49 publications

(42 citation statements)

References 53 publications

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“…8,9 Furthermore, in those studies it was observed that glycerol is depleted from the surface. This "preferential hydration" is also thought to occur in glycerol-water solutions of lysozyme 35,36 and a number of proteins, 37 but we suggest this is not the case here in the lipid membrane system.…”

Section: Resultsmentioning

confidence: 99%

“…[3][4][5][6][7] By utilizing concurrent surface water diffusivity and equilibrium surface forces measurements, the present work suggests that the two molecules influence membrane hydration differently, with DMSO effectively desolvating the surface and glycerol strengthening surface hydration, but only as much as glycerol increases the bulk water viscosity. Similar comparisons on surface hydration between DMSO and glycerol have been raised in studies on model peptides, largely through neutron scattering measurements, 8,9 but direct comparisons of the effects of these cryoprotectants on lipid membrane systems remain absent.…”

Section: Introductionmentioning

confidence: 99%

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Communication: Contrasting effects of glycerol and DMSO on lipid membrane surface hydration dynamics and forces

Schrader

Cheng

Israelachvili

et al. 2016

The Journal of Chemical Physics

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Water structure around hydrophobic amino acid side chain analogs using different water models The Journal of Chemical Physics 146, 225104 (2017) Glycerol and dimethyl sulfoxide (DMSO) are commonly used cryoprotectants in cellular systems, but due to the challenges of measuring the properties of surface-bound solvent, fundamental questions remain regarding the concentration, interactions, and conformation of these solutes at lipid membrane surfaces. We measured the surface water diffusivity at gel-phase dipalmitoylphosphatidylcholine (DPPC) bilayer surfaces in aqueous solutions containing ≤7.5 mol. % of DMSO or glycerol using Overhauser dynamic nuclear polarization. We found that glycerol similarly affects the diffusivity of water near the bilayer surface and that in the bulk solution (within 20%), while DMSO substantially increases the diffusivity of surface water relative to bulk water. We compare these measurements of water dynamics with those of equilibrium forces between DPPC bilayers in the same solvent mixtures. DMSO greatly decreases the range and magnitude of the repulsive forces between the bilayers, whereas glycerol increases it. We propose that the differences in hydrogen bonding capability of the two solutes leads DMSO to dehydrate the lipid head groups, while glycerol affects surface hydration only as much as it affects the bulk water properties. The results suggest that the mechanism of the two most common cryoprotectants must be fundamentally different: in the case of DMSO by decoupling the solvent from the lipid surface, and in the case of glycerol by altering the hydrogen bond structure and intermolecular cohesion of the global solvent, as manifested by increased solvent viscosity. Published by AIP Publishing.[http://dx

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Communication: Contrasting effects of glycerol and DMSO on lipid membrane surface hydration dynamics and forces

Schrader

Cheng

Israelachvili

et al. 2016

The Journal of Chemical Physics

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“…5 It is a "kosmotropic" agent, believed to increase the ordering of water molecules in the first hydration shell of water dissolved substances. 6,7 An important property for the present study is that DMSO affects the dynamics of the hydration layer even at bulk concentrations (0:1% À 1 % or 14 À 140 mM) which are too small to affect the properties of the bulk solvent. Presumably, DMSO accumulates into ("binds to") the hydration shell.…”

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confidence: 99%

Nano-rheology measurements reveal that the hydration layer of enzymes partially controls conformational dynamics

Alavi

Ariyaratne

Zocchi

2015

Applied Physics Letters

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For a typical (20 kD, 4 nm size) monomeric enzyme, more than 50% of the residues are at the surface. The mechanics of these soft, heterogeneous nanoparticles was recently shown to be viscoelastic. Here, we explore the contribution of the enzyme's surface to the mechanics of the molecule. Nano-rheology provides sub-Å resolution measurements of the reversible deformation of the enzyme subject to an oscillatory mechanical stress. We perturb the surface of the enzyme by adding small amounts of DMSO (dimethyl sulfoxide), believed to affect ordering of the enzyme–water interface. We observe a dramatic though reversible change in the mechanics of the enzyme, which becomes more viscous. On the other hand, the catalytic speed is unaffected, while at higher DMSO concentrations (>1 %) it even increases.

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“…Our approach in this case is not to use reducing agents at all during this process, or at least at a very low BME concentration (2 mM) as a compromise solution Chaotropic salts: They have a higher ''salting-in'' effect according to the Hofmeister series. On one hand, they are water-structure breakers and protein destabilizers; but on other hand, they can reduce protein-protein interactions by shielding charges and by preventing the stabilization of salt bridges [61,64,79] Detergents: Some detergents disrupt hydrophobic interactions…”

Section: Protein Environmentmentioning

confidence: 99%

“…SEC can be coupled in-line to a light-scattering device (SEC-MALS) to measure the absolute molar mass, size, and shape of macromolecules in solution. One major disadvantage is that it is time consuming, although this can be partially circum- [50,[61][62][63]69,[78][79][80][81] and from commercial websites (DILYX Biotechnologies OptiSol protein solubility screening kit application manual, HAMPTON: Solubility and stability screen).…”

Section: Protein Environmentmentioning

confidence: 99%

Production of prone‐to‐aggregate proteins

Lebendiker¹,

Danieli²

2013

FEBS Letters

129

102

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a b s t r a c tExpression of recombinant proteins in Escherichia coli (E. coli) remains the most popular and costeffective method for producing proteins in basic research and for pharmaceutical applications. Despite accumulating experience and methodologies developed over the years, production of recombinant proteins prone to aggregate in E. coli-based systems poses a major challenge in most research applications. The challenge of manufacturing these proteins for pharmaceutical applications is even greater. This review will discuss effective methods to reduce and even prevent the formation of aggregates in the course of recombinant protein production. We will focus on important steps along the production path, which include cloning, expression, purification, concentration, and storage.

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The impact of kosmotropes and chaotropes on bulk and hydration shell water dynamics in a model peptide solution

Cited by 49 publications

References 53 publications

Communication: Contrasting effects of glycerol and DMSO on lipid membrane surface hydration dynamics and forces

Communication: Contrasting effects of glycerol and DMSO on lipid membrane surface hydration dynamics and forces

Nano-rheology measurements reveal that the hydration layer of enzymes partially controls conformational dynamics

Production of prone‐to‐aggregate proteins

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