Publication Date

9-3-2023

Document Type

Article

Publication Title

Supramolecular Chemistry

DOI

10.1080/10610278.2023.2254442

Abstract

The thermodynamics of model host–guest-binding reactions is examined in depth using isothermal titration calorimetry. In conflict with classical thermodynamics, the results indicate that the equilibrium-binding quotient, K, is not a constant for all pairings. This outcome is predicted by an equation for binding equilibria that includes an explicit term for the change in solvation free energy that accompanies the formation of a binary complex. Application of this framework to the experimentally observed concentration dependence of K allows one to obtain the energetic contribution of the solvent, a linked equilibrium denoted here as ΔGH2O. The estimated values of ΔGH2O are large and unfavourable for the binding of selected guest molecules to two hosts, cucurbit[7]uril and p-sulfonatocalix[4]arene. Intriguingly, the estimated values of ΔGH2O are near zero for the binding of two hydrophobic guest molecules to β-cyclodextrin, leading to a thought-provoking discussion on the driving force behind the hydrophobic effect.

Keywords

Binding thermodynamics, isothermal titration calorimetry, solvation energy, hydration, hydrophobic effect

Comments

This article is discussed in the editorial titled "Constructive Disagreement," by Nicholas G. White (https://doi.org/10.1080/10610278.2023.2270760).

Creative Commons License

Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License.

Department

Chemistry

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Supramolecular Chemistry Dataset Eggers.7z (2697 kB)
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