Thermodynamic Constants of Glycyl Peptides: Solvation and Buffers for the Physiological pH Range

The pK ₂ values for the dissociation of the NH ₃ ⁺ charge center of the glycyl peptides, e.g., glycyl-D-asparagine, glycyl-DL-serine, glycyl-L-leucine, and glycyl-DL-methionine have been determined at 10 temperatures in the range 5–50°C by measurements of the emf of cells without liquid junction, utilizing hydrogen electrodes and silver–silver bromide electrodes. The thermodynamic quantities, H ^o, C _p ^o and S ^o were calculated from the temperature coefficients of the dissociation constants. The pK ₂ values at 25°C are 8.268 (glycyl-D-asparagine), 8.277 (glycyl-DL-serine), 8.323 (glycyl-L-leucine), and 8.408 (gly-cyl-DL-methionine). These values show that changes in the substituents on the -carbon atom have very little effect on the dissociation of the NH ₃ ⁺ , with the possible exception of glycyl-DL-methionine. The suitability of these compounds as buffers in the physiologically important pH range 7–9 is of interest. The thermodynamics of the solute–solvent interaction is interpreted in terms of a mixture model. The peptides chosen for study include both polar and nonpolar substituents.