Biophysical methods

Isothermal titration calorimetry (ITC)- is used to directly measure the heat of reaction released or received during chemical reactions, including interactions of biomolecules in solution. At IBP, it is used to determine thermodynamic characteristics of interactions of antitumor metal pharmaceuticals with DNA or proteins.

Differential scanning calorimetry (DSC) - allows you to monitor the thermal changes that occur in biomolecules depending on temperature. The method is used to monitor the stability of the sample in solution and allows to determine thermodynamic parameters describing the state of the studied biomolecules - the measured change in heat capacity and enthalpy allows to determine the change in entropy and total free (Gibs) energy. At IBP, the method is used to study the effect of metallopharmaceutical binding on DNA or proteins.

Microscale thermophoresis (MST) is a method used to measure the thermodynamic properties of particles in solution. This method can quantitatively study the mutual bonding of biomolecules, e.g., the interaction of two strands of DNA in the formation of a double helix, the interaction of DNA-protein, protein-protein, or the interaction of DNA or protein with low molecular weight ligands. A great advantage over related techniques is the low sample consumption and the possibility of measuring KD even with weakly weighing partners. It is also possible to determine binding parameters in complex environments close to in vivo conditions, e.g., cell lysates or serum. At IBP, the method is used to study the interactions of biologically active substances with DNA.