THERMODYNAMICS OF STEPWISE DISSOCIATION OF GLYCYL-D-PHENYLALANINE IN AQUEOUS SOLUTION

• Published in: ChemChemTech Vol. 67; no. 2; pp. 6 - 12
• Format: Journal Article
• Language: English
• Published: 2024
• ISSN: 0579-2991; 2500-3070
• DOI: 10.6060/ivkkt.20246702.6882

Recently, more and more drugs that are derivatives of oligopeptides have been introduced to the pharmaceutical market. The structural elements of these compounds are amino acids and dipeptides. When stabilizing functional groups are introduced into the peptide structure, as well as through the use of special delivery systems, oligopeptide derivatives can be used as innovative medicines. The calorimetric method was used to determine the heat of interaction of glycyl-D-phenylalanine with solutions of nitric acid and potassium hydroxide at 298.15K and the values of the ionic strength of the solution 0.5, 0.75 and 1.0 in the presence of KNO3. Measurements were carried out on a calorimeter with an isothermal shell and automatic recording of the temperature-time curve. The unit was equipped with a reaction vessel with a volume of 60 cm3. Calibration was performed by current at T = (293.15–308.15) ± 0.01 K and P = 100.5± 0.7 kPa. A thermistor KMT-14 was used as a temperature sensor. The temperature of the calorimetric cell was controlled in a thermostat equipped with a PID controller with an accuracy of 0.002 K. The temperature sensor of the thermostat was a platinum resistance thermometer. The calorimeter was calibrated by current. The volume of the calorimetric liquid is 42.83 ml. The enthalpy of stepwise dissociation of glycyl-D-phenylalanine at zero ionic strength was found by an equation with one individual parameter. Standard thermodynamic characteristics (ΔrH°, ΔrG°, ΔrS°) of acid-base interaction reactions in aqueous solutions of glycyl-D-phenylalanine are calculated. The effect of the background electrolyte concentration on the dissociation heats of glycyl-D-phenylalanine is considered. Knowledge of the thermochemical characteristics of dipeptides is necessary for understanding and subsequent modeling of the process of protein biosynthesis occurring in biological systems. Data on the thermodynamic characteristics of dipeptide solutions are needed in various fields where these compounds are used: pharmacology, medicine, food and cosmetic industries, for the development, justification and optimization of technological processes involving these compounds and their complexes with metals.