Detection of interaction between ornidazole and albumin by using thermodynamic parameters

The binding of 1-chloro-3-(2-methyl-5-nitro-1H-imidazole-1-yl) propan-2-ol (Ornidazole) to human serum albumin (HSA) was studied by fluorescence and UV-visible spectroscopy. Interaction ornidazole (OR) with HSA identified Stern-Volmer Van’t Hoff equations. constant, Kb the thermodynamic parameters, ∆H, ∆S, ∆G at different temperatures were calculated several Data shows that quenching mechanism may occur via static quenching. parameters showed van der Waals interactions hydrogen bonds are major forces for interaction HSA. spectral changes synchronous suggested both microenvironment OR conformation concerning their concentrations have changed during binding.