Binding of hydrophobic fluorinated bisphenol A to large unilamellar vesicles of egg phosphatidylcholine.

The kinetics of membrane binding and dissociation of fluorinated bisphenol A (FBPA, (CF(3))(2)C(C(6)H(4)OH)(2)) is quantified by 1D (19)F NMR spectra in situ. Although the bound and free components are in fast exchange, the rate constants and bound fraction is nonetheless determined from an analysis of the spectra. The analysis relies on the expression of 1D NMR signal intensity by a set of Bloch equations with exchange terms. The time span of the binding and dissociation of hydrophobic FBPA to large unilamellar vesicles of egg phosphatidylcholine (EPC) is 10(-3) to 10(-2) s. The rates of FBPA binding and dissociation are kept constant per EPC molecule even at different concentrations of the vesicle. The free energy of FBPA transfer is -20 ± 2 kJ/mol at 303 K. The process is entropy-driven. The efficiency of FBPA transfer is enhanced by a factor of 7 × 10(4), as compared with the hydrophilic 5-fluorouracil.