Journal of Physical Chemistry, Vol.100, No.6, 2447-2455, 1996
Enthalpy-Entropy Compensation in Hydrophobic Interaction Chromatography
Exothermodynamic relationships between thermodynamic quantities and molecular structure are employed to facilitate a molecular interpretation of enthalpy-entropy compensation (EEC). For hydrophobic interactions the compensation temperature T-C is expressed in terms of the enthalpy and entropy change, both per unit nonpolar surface area of the molecules, and it is concluded that the utility of T-C as a diagnostic tool for the mechanistic identity of processes rests on this simple dependence of T-C on molecular parameters. Whereas classical EEC is observed only with processes involving no heat capacity change and T-C is evaluated from the slopes of linear enthalpy versus entropy plots of data measured at any temperature, this investigation shows that even when the heat capacity change is finite and constant or varies linearly with the temperature, EEC can occur with processes if they are subject to the same mechanism at a fixed temperature. Tn turn, the compensation temperature changes with the experimental temperature, reflecting mechanistic changes as expected with processes such as hydrophobic interaction chromatography that are governed by hydrophobic interactions and driven by entropy or enthalpy change at low or high temperatures. These compensating processes exhibit at least one isoenergetic temperature T-G*, which marks the intersection point of curved van’t Hoff plots, where all species have the same free energy change in the same way as at T-C in the case of linear van’t Hoff plots. In turn, the isoenthalpic T-H* and isoentropic T-S* temperatures mark the intersection points of the respective plots of enthalpy and entropy versus temperature as described in the literature. The triad of isothermodynamic temperatures is characteristic for processes which can be represented by constant heat capacity change and evince compensation behavior.
Keywords:REVERSED-PHASE CHROMATOGRAPHY;PROTEIN-FOLDING THERMODYNAMICS;SOLID CYCLIC DIPEPTIDES;CAVITY SURFACE-AREA;MOLAR HEAT-CAPACITY;LIQUID-CHROMATOGRAPHY;GASEOUS HYDROCARBONS;ELUENT COMPOSITION;AQUEOUS-SOLUTION;WATER