Handbook of Aqueous Solubility Data

Yalkowsky, Samuel H.; He, Yan; Jain, Parijat

doi:10.1201/9780203490396

Cited by 357 publications

(299 citation statements)

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“…In contrast to the temperature dependence of macroscopic interfacial free energy, ΔG hyd for a hydrophobic solute increases at low temperature, reaches a maximum and decreases at high temperature. This temperature dependence has been observed for small hydrocarbon molecules (36), and has been reproduced by many theoretical studies (19,21,23,28). This anomalous increase in the hydration free energy before the turnover point is believed to originate from the lowered entropy of water molecules adjacent to the small hydrophobic molecules, as the degrees of freedom of these water molecules are reduced by the formation of more ordered, dynamic structures.…”

Section: Resultsmentioning

confidence: 52%

Signature of hydrophobic hydration in a single polymer

Walker

2011

Proc. Natl. Acad. Sci. U.S.A.

156

158

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Hydrophobicity underpins self-assembly in many natural and synthetic molecular and nanoscale systems. A signature of hydrophobicity is its temperature dependence. The first experimental evaluation of the temperature and size dependence of hydration free energy in a single hydrophobic polymer is reported, which tests key assumptions in models of hydrophobic interactions in protein folding. Herein, the hydration free energy required to extend three hydrophobic polymers with differently sized aromatic side chains was directly measured by single molecule force spectroscopy. The results are threefold. First, the hydration free energy per monomer is found to be strongly dependent on temperature and does not follow interfacial thermodynamics. Second, the temperature dependence profiles are distinct among the three hydrophobic polymers as a result of a hydrophobic size effect at the subnanometer scale. Third, the hydration free energy of a monomer on a macromolecule is different from a free monomer; corrections for the reduced hydration free energy due to hydrophobic interaction from neighboring units are required.H ydrophobic hydration involves the minimization of the free energies of water molecules near nonpolar surfaces. Hydrophobic hydration of macromolecules is central to understanding protein folding (1-6) and advancing materials science and biotechnologies (7-9). A detailed methodology has been developed to study hydrophobic hydration by the mechanical unfolding of a collapsed single hydrophobic polymer (10). Typically, the hydration free energy (ΔG hyd ) is assumed to scale with the solvent accessible surface area (SASA) of molecules according to macroscopic interfacial thermodynamics, which is supported by the linear correlation between the SASA and the free energy to transfer hydrocarbons from a hydrophobic solvent (such as hexadecane) to water (11). Despite a strong correlation, the experimentally measured small hydrocarbon ΔG hyd is smaller than that predicted by the calculated SASA (12), showing the breakdown of macroscopic interfacial thermodynamics at the microscopic scale and suggesting that the origin of the correlation goes beyond SASA. In addition, the temperature dependence of ΔG hyd (the signature of hydrophobic hydration) varies according to the size of the solute; such temperature dependence cannot be explained simply by the macroscopic interfacial free energy. In an earlier attempt to address these issues, Tolman (13) developed a thermodynamic treatment that lowers the surface tension of water at the solutewater interface by taking into account the cavity curvature. Later developments included temperature dependence of the Tolman length using simulations to address the temperature dependence of ΔG hyd (14, 15). However, it was argued that the correction to the effective surface tension to maintain the correlation between ΔG hyd and SASA at small length scales lacked a clear physical meaning (16). Instead of depending on a scaling relation with SASA, theories and simulations were developed predic...

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Section: Resultsmentioning

confidence: 52%

Signature of hydrophobic hydration in a single polymer

Walker

2011

Proc. Natl. Acad. Sci. U.S.A.

156

158

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“…About 6 % of the log S measurements were done at two temperatures, each result reported from a different laboratory ("n=2, different labs" set), potentially representing the leastreliable slope-calculated enthalpy values. By contrast, in 73 % of the studies, all of the temperature-dependent log S measurements for a given molecule come from the same laboratory (e.g., the curated "653-set" from the Yalkowsky et al handbook [8]). The latter "one source" temperature-solubility data are expected to lead to the most-reliable calculated enthalpy values.…”

Section: Methodsmentioning

confidence: 99%

“…Figure 3 illustrates the impact of normalizing intrinsic solubility data to the 25 °C benchmark temperature. Figure 3a represents high-quality solubility measurements from the Yalkowsky et al [8] handbook, albeit of relatively simple molecules. The interlaboratory errors are reduced 7.8-fold on the average, to an average value SD(25 °C) = 0.06 log unit.…”

Section: Interlaboratory Errors Temperature Effectmentioning

confidence: 99%

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Solubility Temperature Dependence Predicted from 2D Structure

Avdeef

2015

ADMET DMPK

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“…It is recommended that solubility be tabulated both in molarity and in practical (mg/mL) units, as done in the Handbook of Aqueous Solubility Data (Yalkowsky et al [152]). Standard deviations in the measured solubility (based on averaging three or more values) should be included in the table of values.…”

Section: Recommendation For Reporting Solubility Unitsmentioning

confidence: 99%