Spectroscopic investigation of tolmetin interaction with human serum albumin

- Tolmetin interaction with human serum albumin (HSA) was analyzed by steady state and time resolved fluorescence spectroscopy.
- Results show ligand-HSA complex formation with 1:1 stoichiometry. The binding constants Ka was calculated for 25, 37 and 47 °C.
- The association process was exothermic (ΔH0 < 0), predominantly enthalpy driven.
- Quenching efficiency calculations, based on steady-state and time-resolved fluorescence spectroscopy, indicate that both static and dynamic quenching mechanisms are present.