Modeling of Thermodynamic Properties of Amino Acids and Peptides Using Additivity and HKF Theory

Abstract

Relative densities, \(\left( {\rho - \rho _o } \right)\), and heat capacity ratios, \([(c_p \rho /c_{p1}^o \rho _o ) - 1],\) of aqueous L-histidine, L-phenylalanine, L-tyrosine, L-tryptophan, and L-2,3-dihydroxyphenylalanine (L-dopa) have been measured at 15, 25, 40, and 55°C and 0.1 MPa. Apparent molar volumes, V2,Φ, apparent molar heat capacities, CP2,Φ, partial molar volumes at infinite dilution,\(V_2^o\), and partial molar heat capacities at infinite dilution, \(V_{p2}^o\), have been calculated from these measurements and compared to available literature values. The partial molar properties at infinite dilution for these systems have been added to those previously obtained for amino acids and peptides in water and the combined set used as input to a novel additivity analysis. The model we develop is based upon the equations of state of Helgeson, Kirkham, and Flowers (HKF) and has been constructed with additive parameters. The model may be used to predict thermodynamic properties of many aqueous biochemicals over an extended temperature range. Group contributions to the parameters in our model and effective Born coefficients are reported for 24 aqueous amino acid and peptide systems. Our results are compared to data previously published in the literature.