Abstract
The thermodynamic functions that describe the complexation of a series of four carboxylic acid guests and two related quaternary ammonium derivatives with β-cyclodextrin were measured using flow calorimetry at 298 K in aqueous media in the presence and in the absence of large concentrations of urea. The relative differences of the thermodynamic parameters of complexation revealed the existence of specific interactions between urea and the aromatic surfaces of some of the nonpolar guests. As expected, the relative changes in the complex stability constants upon addition of urea have been found to depend on the balance of opposing enthalpic and entropic contributions. The interpretation as well as the magnitude of the interaction between urea and aromatic surfaces are in line with previous experimental and computational studies. The experimental evidence presented in this work provides insight into the mechanism by which large amounts of urea denature globular proteins in aqueous media.
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