[Microcalorimetric study of the parameters of dicloxacillin binding with human serum albumin at different temperatures].

The thermodynamic parameters of human serum albumin (HSA) binding with dicloxacillin, an antibiotic widely used in clinical practice, were determined with the method of differential flow microcalorimetry at 18, 25, 30, 37 and 45 degrees C. The experiments were performed at two ionic strengths: 0.02 and 0.15. Two hypothetic models of interaction in the HSA-drug system were considered in processing the data for the curves of calorimetric titration. The first model implies the presence of independent homogeneous active sites on the protein. In accordance with the second model there are one primary and secondary independent homogeneous active sites on the biopolymer molecule. It is shown that dicloxacillin association with HSA proceeds according to the mechanism suggesting the presence of one primary and one secondary active sites on the protein molecule. The binding process in the system studied is exothermic, the enthalpy increasing at the temperature change from 18 to 45 degrees C. At the same time the binding constant and enthropy of the system decrease. The influence of the solution ionic strength on the binding process was practically lacking. On the basis of the analysis of the thermodynamic data it is concluded that the character of the binding in the HSA-dicloxacillin system at 18-30 degrees C is hydrophobic. With an increase in the temperature the hydrophoby level decreases.