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Here we introduce a new technique that probes voltage-dependent charge displacements of excitable membrane-bound proteins using extracellularly applied radio frequency (RF, 500 kHz) electric fields.  Xenopus  oocytes were used as a model cell for these experiments, and were injected with cRNA encoding  Shaker  B-IR ( Sh B-IR) K +  ion channels to express large densities of this protein in the oocyte membranes. Two-electrode voltage clamp (TEVC) was applied to command whole-cell membrane potential and to measure channel-dependent membrane currents. Simultaneously, RF electric fields were applied to perturb the membrane potential about the TEVC level and to measure voltage-dependent RF displacement currents.  Sh B-IR expressing oocytes showed significantly larger changes in RF displacement currents upon membrane depolarization than control oocytes. Voltage-dependent changes in RF displacement currents further increased in  Sh B-IR expressing oocytes after ∼120 µM Cu 2+  addition to the external bath. Cu 2+  is known to bind to the  Sh B-IR ion channel and inhibit  Shaker  K +  conductance, indicating that changes in the RF displacement current reported here were associated with RF vibration of the Cu 2+ -linked mobile domain of the  Sh B-IR protein. Results demonstrate the use of extracellular RF electrodes to interrogate voltage-dependent movement of charged mobile protein domains — capabilities that might enable detection of small changes in charge distribution associated with integral membrane protein conformation and/or drug–protein interactions.

Monitoring Voltage-Dependent Charge Displacement of Shaker B-IR K+ Ion Channels Using Radio Frequency Interrogation