Thermodynamic characteristics of molecular interactions between L-tryptophan and nicotinic acid and uracyl in aqueous buffer solutions at 298 K

Abstract

The interaction between L-tryptophan (Trp) and nicotinic acid (NA) and uracyl (Ur) in aqueous buffer solutions (pH 7.35) at different ratios of reagents is studied via the calorimetry of dissolution. The enthalpies of dissolution of the amino acid in the buffer solutions of the ligands at 298.15 K are obtained. The stoichiometric compositions of the complexes being formed and binding constants have been determined. The values of the thermodynamic characteristics for the complex formation of L-tryptophan with nicotinic acid and uracyl are calculated. It is shown that the formation of molecular complexes with 1 : 2 composition is stabilized by the entropy factor for the Trp–NA system, and by the enthalpy factor for the Trp–Ur system.