Evaluating the interaction between di-fluorinated chalcones and plasmatic albumin

The spectroscopic values indicate that di-fluorinated chalcones bind moderatelly to BSA. It does not affect the secondary structure of the albumin and the thermodynamic parameters are favourable for the binding process. The molecular docking suggests Trp-212-containing binding site as the main binding site for the interaction. Theoretical methods showed that changing the fluorine atoms from ring A (connected to the double bond) to ring B (connected to the carbonyl group) in the fluorinated chalcones did not change their binding ability.