AI Article Synopsis
- Researchers studied ion channels made from p-octiphenyls with amphiphilic, cationic tripeptide strands, examining two versions: one with an axial dipole moment (5) and one without (6).
- The channels exhibited voltage dependence and anion selectivity in fluorescence tests and conductance measurements, with 5 forming short-lived channels that could transition into stable structures.
- Studies confirmed that membrane potentials influenced the ability of compound 5 to integrate into bilayers, suggesting that this integration is dependent on voltage.
Article Abstract
Ion channels formed by p-octiphenyls equipped with amphiphilic, cationic tripeptide strands and either with (5) or without (6) axial dipole moment are described (preliminary communication: N. Sakai, S. Matile, J. Am. Chem. Soc. 2002, 124, 1184-1185). Fluorescence kinetics with variably polarized neutral or anionic vesicles, together with planar bilayer conductance measurements, reveal voltage dependence with weakly lyotropic anion selectivity, and deactivation by competing surface potentials of the ion channels formed by asymmetric 5. In planar bilayers, 5 forms short-lived, poorly organized channels--similar to those produced by alpha-helical natural antibiotics--capable of transforming into stable, ohmic p-octiphenyl "beta-barrel" ion channels similar to those of the >99 % homologous but symmetric 6. Fluorescence depth quenching and circular dichroism studies confirm the effect of membrane potentials in promotion of the partitioning of 5 (but not 6) into the bilayers, identifying partitioning as the voltage-dependent step.
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| http://dx.doi.org/10.1002/chem.200390016 | DOI Listing |
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