Modulation of action potentials using PEDOT:PSS conducting polymer microwires.

We describe the use of PEDOT:PSS conducting polymer microwires to modulate action potentials in single cells. PEDOT: PSS conducting polymer microwires are electrochemically synthesized with diameters ranging from 860 nm to 4.5 µm and conductivities of ~30 S/cm. The length of the microwires is controlled by the spacing of the electrodes used for the electrochemical polymerization. We demonstrate the use of these microwires to control the action potentials of cardiomyocytes, showing that the cellular contractions match the frequency of the applied voltage. Membrane integrity assays confirm that the voltage delivered by the wires does not damage cells. We expect the conducting polymer microwires will be useful as minimally invasive devices to control the electrical properties of cells with high spatial precision.

Controlling the Resting Membrane Potential of Cells with Conducting Polymer Microwires.

All cells have a resting membrane potential resulting from an ion gradient across the plasma membrane. The resting membrane potential of cells is tightly coupled to regeneration and differentiation. The ability to control this parameter provides the opportunity for both biomedical advances and the probing of fundamental bioelectric pathways. The use of poly(3,4-ethylenedioxythiophene): polystyrene sulfonate (PEDOT:PSS) conducting polymer microwires to depolarize cells is tested using E. coli cells loaded with a fluorescent dye that is pumped out of the cells in response to depolarization; a more positive membrane potential. Fluorescence imaging of the cells in response to a conducting-polymer-microwire applied voltage confirms depolarization and shows that the rate of depolarization is a function of the applied voltage and frequency. Microwire activity does not damage the cells, demonstrated with a propidium iodide assay of membrane integrity. The conducting polymer microwires do not penetrate the cell, or even come into contact with the cell; they only need to generate a minimum electric field, controlled by the placement of the wires. It is expected that these microwires will provide a new, noninvasive, cellular-scale tool for the control of resting membrane potential with high spatial precision.

Conducting polymer nanowires for control of local protein concentration in solution.

Interfacing devices with cells and tissues requires new nanoscale tools that are both flexible and electrically active. We demonstrate the use of PEDOT:PSS conducting polymer nanowires for the local control of protein concentration in water and biological media. We use fluorescence microscopy to compare the localization of serum albumin in response to electric fields generated by narrow (760 nm) and wide (1.5 µm) nanowires. We show that proteins in deionized water can be manipulated over a surprisingly large micron length scale and that this distance is a function of nanowire diameter. In addition, white noise can be introduced during the electrochemical synthesis of the nanowire to induce branches into the nanowire allowing a single device to control multiple nanowires. An analysis of growth speed and current density suggests that branching is due to the Mullins-Sekerka instability, ultimately controlled by the roughness of the nanowire surface. These small, flexible, conductive, and biologically compatible PEDOT:PSS nanowires provide a new tool for the electrical control of biological systems.

Quartz crystal microbalance study of bovine serum albumin adsorption onto self-assembled monolayer-functionalized gold with subsequent ligand binding.

Adsorption characteristics of the model protein bovine serum albumin (BSA) onto gold surfaces were examined using a 5 MHz quartz crystal microbalance. Protein immobilization was executed in the presence and absence of a homogenous self-assembled monolayer (SAM) of NHS-terminated alkanethiols. BSA concentrations in the range of 3.2 × 10(-6) to 1.0 × 10(-3)mol/L were found to saturate both SAM-functionalized and non-functionalized surfaces with similar densities of 450 ± 26 ng/cm(2). The lack of functionalization dependence is attributed to the large protein size relative to the density of available binding sites in either surface condition. The BSA ligand 8-anilino-1-naphthalenesulfonic acid (ANS) was subsequently introduced to the immobilized BSA to determine any effects of the protein immobilization conditions on ligand binding. The rate of ANS binding to BSA was found to increase with increasing BSA concentration used in the immobilization step. This suggests that protein concentration affects morphology and ligand binding affinity without significantly altering adsorption quantity.