INTERACTION OF L-CARNOSINE WITH NICOTINIC AND ISONICOTINIC ACIDS IN AQUEOUS SOLUTIONS AT 298.15 K

Abstract

Understanding the mechanism of interaction of drugs with proteins has drawn attention of numerous researchers. The thermodynamic investigations of liquid-phase systems containing peptide and drug make it possible to determine the nature and driving forces of the interaction between them. In this work, we present results of interaction study of peptide L-carnosine (Car), as model of polypeptide chains in protein, with isonicotinic and nicotinic acids, as the drug models, in aqueous solution using calorimetric method. Calorimetric measurements of the enthalpy of L-carnosine dissolution in water and aqueous solutions with two isomers of pyridine carboxylic acid additives were performed on an ampoule-type isoperibolic dissolution calorimeter at 298.15 K. The error of measuring single heat effects was below 0.2%. The relative combined uncertainty in the measurements of the enthalpies of dissolution was not more than 0.7%. Based on the obtained experimental data and the using the HEAT computer program, the thermodynamic parameters (lgKc, ΔcG, ΔcH, ΔcS) of the complex formation between the reagents were calculated. A comparison of the affinity of peptide to interaction with nicotinic acid and isonicotinic acid was carried out. It is shown that the interaction of L-carnosine with isonicotinic acid leads to the formation of a more stable complex than with nicotinic acid. This fact may be mainly explained by the changing of ionic state of the reagents in solution and the predominance of the zwitterionic forms of isonicotinic acid in compared with nicotinic acid. The data obtained reveal the presence of molecular complexes between Car and isomers of pyridine carboxylic acid with 1:2 stoichiometry in aqueous solutions. The complexes of Car with the isonicotinic acid are mainly enthalpically stabilized, while those of Car with nicotinic acid are stabilized by both enthalpic and entropic contributions to the free Gibbs energy. The main interactions in complexes stabilization are believed to be electrostatic forces and hydrogen bonds formation between peptide and pyridine monocarboxylic acids. For citation: Tyunina E.Yu., Mezhevoi I.N., Barannikov V.P. Interaction of L-carnosine with nicotinic and isonicotinic acids in aqueous solutions at 298.15 K. ChemChemTech [Izv. Vyssh. Uchebn. Zaved. Khim. Khim. Tekhnol.]. 2024. V. 67. N 7. P. 48-54. DOI: 10.6060/ivkkt.20246707.7010.