Recent developments in the theoretical, simulational, and experimental studies of the role of water hydrogen bonding in hydrophobic phenomena

Djikaev, Y. S.; Ruckenstein, Eli

doi:10.1016/j.cis.2016.05.006

Cited by 13 publications

(7 citation statements)

References 145 publications

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“…Both, the hydrophobic and hydrophilic solvation depend on thermodynamic conditions of the solvent (e.g., pressuretemperature). 51 Thus, changes in the free energy of the system are due to structural and energetic changes in the solvent around each solute molecule, 51,52 and hence, water molecules exhibits a preferred orientation at the hydrophilic or hydrophobic surface. 53 This is linked to the result of Djikaev and Ruckenstein, 51 who computed the effective width of the fluid solvent-solute transition layer (σ) and average density (ρ) therein, where the behavior change of σ and ρ modifies the hydration mechanism depending on the solute-solvent affinity.…”

Section: Discussionmentioning

confidence: 99%

The role of hydrophobicity in the cold denaturation of proteins under high pressure: A study on apomyoglobin

Espinosa

Caffarena

Grigera

2019

The Journal of Chemical Physics

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An exciting debate arises when microscopic mechanisms involved in the denaturation of proteins at high pressures are explained. In particular, the issue emerges when the hydrophobic effect is invoked, given that hydrophobicity cannot elucidate by itself the volume changes measured during protein unfolding. In this work, we study by the use of molecular dynamics simulations and essential dynamics analysis the relation between the solvation dynamics, volume, and water structure when apomyoglobin is subjected to a hydrostatic pressure regime. Accordingly, the mechanism of cold denaturation of proteins under high-pressure can be related to the disruption of the hydrogen-bond network of water favoring the coexistence of two states, low-density and high-density water, which directly implies in the formation of a molten globule once the threshold of 200 MPa has been overcome.

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Section: Discussionmentioning

confidence: 99%

The role of hydrophobicity in the cold denaturation of proteins under high pressure: A study on apomyoglobin

Espinosa

Caffarena

Grigera

2019

The Journal of Chemical Physics

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“…The principal solvent of nature is water, which is the protagonist of hydrophobic effects. − Their wide momentousness is exemplified in a variety of phenomena in natural, engineering, and pharmaceutical sciences, such as self-assembly of amphiphilic molecules to biological membranes, , receptor–ligand binding, ,− catalysis using cavitands, − transport through nanopores, − as well as protein folding, stability, and function. − Having a common foundation in the incompatibility of water and nonpolar solutes, the hydrophobic effects are quite diverse in their physical nature. In particular, they exhibit a characteristic length scale dependence, which is a consequence of the different water structure, dynamics, and fluctuations around small and large hydrophobic objects − and leads to an exchange between enthalpic and entropic thermodynamic driving forces …”

Section: Introductionmentioning

confidence: 99%

“…Non-polar solutes are usually classified as hydrophobic (Attic Greek: hýdrofor "water" and phóbos for "fear"). The verbalism "hydrophobic effect" gathers the consequences of hydrophobicity that dictate the driving forces for macromolecular conformations and association processes like the aforementioned micelle formation and molecular recognition [7][8][9][10][11].…”

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confidence: 99%

Principles for Tuning Hydrophobic Ligand–Receptor Binding Kinetics

Weiß

Setny

Dzubiella

2017

J. Chem. Theory Comput.

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We investigate how to tune the rate of hydrophobic ligand-receptor association due to the role of solvent in adjustable receptor pockets by explicit-water molecular dynamics (MD) simulations. Our model considers the binding of a spherical ligand (key/guest) to a concave surface recess in a nonpolar wall as receptor (lock/host). We systematically modify the receptor's physicochemical properties in terms of geometry and dispersion attraction which, in turn, alter the water occupancy and fluctuations within the pocket. We demonstrate that even minor pocket modifications can lead to a significant acceleration of the water-mediated association. For example, the binding switches from comparably slow to fast if the binding pocket becomes only slightly deeper. We find that the degree of hydrophobicity, characterized by hydration occupancy and its fluctuations, clearly correlates with the binding times and, for instance, links the sudden acceleration to an abrupt increase in hydrophobicity. For a deeper analysis based on passage time theory, we quantify the intimate coupling between solvent fluctuations and the ligand's local dynamics and friction. The coupling exhibits substantial nonequilibrium effects and maximizes shortly before binding, which slows down the binding kinetics in all cases. In summary, we rationalize how the physicochemical properties of a nonpolar, concave binding site tune key-lock binding kinetics due to water-mediated forces and fluctuations. Our study thus complements the profound understanding of the solvent's influence in host-guest binding, which is essential for tailored solutions in catalysis and pharmaceutical applications.

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“…10−12 From a thermodynamic point of view, the hydrophobic effect is related to the Gibbs energy of transferring a nonpolar solute into water. 13 The hydrophobic effect is the most important contribution in the classical aggregation formation models developed by Nagarajan and Ruckenstein 14,15 as well as by Blankschtein et al 16−19 These models 14−19 provide an analytical expression for the Gibbs energy of solutions containing water, surfactant molecules, and aggregates of different aggregation sizes and shapes. Although they 14−19 follow the same concept, the detailed expressions differ from each other.…”

Section: Introductionmentioning

confidence: 99%

“…In general, the self-assembly of surfactants in an aqueous environment is of high importance in the chemical process industry, for pharmaceutical and cosmetic applications as well as for consumer products and food processing. The most important driving force for the self-aggregation is the so-called hydrophobic effect also causing the limited solubility of nonpolar molecules in water. − From a thermodynamic point of view, the hydrophobic effect is related to the Gibbs energy of transferring a nonpolar solute into water . The hydrophobic effect is the most important contribution in the classical aggregation formation models developed by Nagarajan and Ruckenstein , as well as by Blankschtein et al − These models − provide an analytical expression for the Gibbs energy of solutions containing water, surfactant molecules, and aggregates of different aggregation sizes and shapes.…”

Section: Introductionmentioning

confidence: 99%

Application of PC-SAFT and DGT for the Prediction of Self-Assembly

Reinhardt¹,

Haarmann

Sadowski

et al. 2020

J. Chem. Eng. Data

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The self-assembly of a surfactant in water is a complex procedure. The classical thermodynamic model for aqueous solutions of a nonionic surfactant, originally developed by Nagarajan and Ruckenstein, includes four contributions for aqueous solutions of a nonionic surfactant. These contributions were calculated using correlations based on experimental data, which were available at that time. The most important contribution is the so-called transfer term for modeling the hydrophobic effect. In this work, we first suggest replacing the original term based on experimental vapor–liquid equilibrium data by the n-alkane activity coefficient at infinite dilution in water calculated with PC-SAFT. The second term in the original model describes the newly formed interface during the self-assembly. This contribution requires the interfacial tension of n-alkane + water mixtures, which was originally calculated using combining rules based on the surface tensions of pure water and pure n-alkane. The second new suggestion of this work is to replace this combining rule by the interfacial tension of n-alkane + water mixtures obtained from PC-SAFT combined with the density gradient theory. The impact of these modifications on the predicted physical properties of surfactant solutions is studied for aqueous solutions of n-octyl-β-d-glucopyranoside (C8G1) as a representative surfactant for the family of sugar surfactants.

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Recent developments in the theoretical, simulational, and experimental studies of the role of water hydrogen bonding in hydrophobic phenomena

Cited by 13 publications

References 145 publications

The role of hydrophobicity in the cold denaturation of proteins under high pressure: A study on apomyoglobin

The role of hydrophobicity in the cold denaturation of proteins under high pressure: A study on apomyoglobin

Principles for Tuning Hydrophobic Ligand–Receptor Binding Kinetics

Application of PC-SAFT and DGT for the Prediction of Self-Assembly

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