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Influence of Anions and Cations on the Dipole Potential of Phosphatidylcholine Vesicles: A Basis for the Hofmeister Effect

MPG-Autoren
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Clarke,  Ronald J.
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Lüpfert,  Christian
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Zitation

Clarke, R. J., & Lüpfert, C. (1999). Influence of Anions and Cations on the Dipole Potential of Phosphatidylcholine Vesicles: A Basis for the Hofmeister Effect. Biophysical Journal, 76(5), 2614-2624. doi:10.1016/S0006-3495(99)77414-X.


Zitierlink: https://hdl.handle.net/21.11116/0000-0007-1DAC-8
Zusammenfassung
Anions and cations have long been recognized to be capable of modifying the functioning of various membrane-related physiological processes. Here, a fluorescent ratio method using the styrylpyridinium dyes, RH421 and di-8-ANEPPS, was applied to determine the effect of a range of anions and cations on the intramembrane dipole potential of dimyristoylphosphatidylcholine vesicles. It was found that certain anions cause a decrease in the dipole potential. This could be explained by binding within the membrane, in support of a hypothesis originally put forward by A. L. Hodgkin and P. Horowicz [1960, J. Physiol. (Lond.) 153:404–412.] The effectiveness of the anions in reducing the dipole potential was found to be ClO4 > SCN > I > NO3 > Br > Cl > F > SO42−. This order could be modeled by a partitioning of ions between the membrane and the aqueous phase, which is controlled predominantly by the Gibbs free energy of hydration. Cations were also found to be capable of reducing the dipole potential, although much less efficiently than can anions. The effects of the cations was found to be trivalent > divalent > monovalent. The cation effects were attributed to binding to a specific polar site on the surface of the membrane. The results presented provide a molecular basis for the interpretation of the Hofmeister effect of lyotropic anions on ion transport proteins.