Application of the ¹⁹F NMR Technique to Observe Binding of the General Anesthetic Halothane to Human Serum Albumin

Abstract

¹⁹F NMR techniques were employed to characterize the binding property of the widely used general anesthetic halothane with human serum albumin (HSA). It was found that ¹⁹F{¹H} NOE and 2D ¹H-¹⁹F HOESY experiments detected intermolecular NOEs between halothane ¹⁹F and HSA protons. Measurements of the diffusion coefficients for halothane were also carried out by ¹H and ¹⁹F NMR, indicating the interaction of halothane with HSA. The present results indicate that these techniques are very suitable to identify a fluorine-containing ligand binding with a protein receptor in the drug-discovery process.