Open AccessCOMPARISON OF L-ASPARAGINE INTERACTIONS WITH PYRIDINE DERIVATIVES, PYRIDOXAL- 5'-PHOSPHATE AND PYRIDOXINE, IN AQUEOUS SOLUTIONS: THERMODYNAMIC ASPECTS
Author(s) -
E. Yu. Tyunina,
О. Н. Крутова,
А. И. Лыткин
Publication year - 2021
Publication title -
izvestiâ vysših učebnyh zavedenij. himiâ i himičeskaâ tehnologiâ/izvestiâ vysših učebnyh zavedenij. seriâ himiâ i himičeskaâ tehnologiâ
Language(s) - English
Resource type - Journals
eISSN - 2500-3070
pISSN - 0579-2991
DOI - 10.6060/ivkkt.20216405.6373
Subject(s) - chemistry , aqueous solution , enthalpy , asparagine , hydrogen bond , pyridoxine , phosphate , dissolution , organic chemistry , inorganic chemistry , molecule , thermodynamics , enzyme , biochemistry , physics
Interactions of proteins with various biologically active substances (hormones, drugs, enzymes, etc.) underlie many biochemical processes in the body. As part of the long-term task to studying various aspects of the interaction between model protein compounds and heterocyclic compounds that are into the structure of many enzymes and drugs, the thermochemical study of aqueous solutions containing aspartic acid amide (L-asparagine) and peridoxal-5¢-phosphate was carried out. Calorimetric measurements of the enthalpy of L-asparagine dissolution in an aqueous solution with pyridoxal-5¢-phosphate 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 binding constants and thermodynamic parameters (lgK, ΔcG, ΔcH, ΔcS) of the complex formation between the reagents under study were calculated. A comparison of the affinity of amino acids to interaction with pyridoxal-5¢-phosphate and pyridoxine was carried out. The features of their behavior in an aqueous solution are revealed. It is shown that the interaction of L-asparagine with pyridoxine leads to the formation of a more stable complex than with peridoxal-5¢-phosphate. This fact may be explained in terms of a bulky phosphate group that hinders apparently the interaction of POP with aspartic acid amide. In addition, the peridoxal-5¢-phosphate molecule contains intramolecular hydrogen bonds between aldehyde CHO and phenolic OH groups, which must be destroyed by the interaction of peridoxal-5' - phosphate with an amino acid, which requires additional energy expenses. Thus, the selectivity of the interaction and the stability of the formed complexes are mainly regulated by the factors of structural and energy complementarity.