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1 H/ 19 F NMR-based screening methods were applied to a human serum albumin-fleroxacin complex. Fleroxacin contains three fluorine atoms in a molecule, which is suitable as a model fluorinated compound for NMR analysis with 1 H and 19 F detection. The 19 F{ 1 H} and 1 H{ 1 H} saturation transfer difference spectra were acquired and the 1 H/ 19 F spin-lattice relaxation rates were measured with and without any selective irradiation of protein resonance to identify the binding epitopes of fleroxacin. Because several 1 H signals of fleroxacin resonated close to water, its precise signal intensities were unavailable. The 19 F NMR-based screening methods successfully provide complementary information, indicating its importance in the analysis of fluorinated compounds.

Identification of Binding Epitopes of a Fluorinated Compound Bound to Proteins Using 1H and 19F NMR Spectroscopy