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D O Wipf

Publications and source records attributed to D O Wipf.

4 recordsLinked to original sources

Impedance feedback control for scanning electrochemical microscopy.

A new constant-distance imaging method based on the relationship between tip impedance and tip-substrate separation has been developed for the scanning electrochemical microscope. The tip impedance is monitored by application of a high-frequency ac voltage bias between the tip and auxiliary electrode. The high-frequency ac current is easily separated from the dc-level faradaic electrochemistry with a simple RC filter, which allows impedance measurements during feedback or generation/collection experiments. By employing a piezo-based feedback controller, we are able to maintain the impedance at a constant value and, thus, maintain a constant tip-substrate separation. Application of the method to feedback and generation/collection experiments with tip electrodes as small as 2 microm is presented.

Journal Article↗

Conductivity detection for monitoring mixing reactions in microfluidic devices.

A conductivity detector was coupled to poly(dimethylsiloxane)-glass capillary electrophoresis microchips to monitor microfluidic flow. Electroosmotic flow was investigated with both conductivity detection (CD) and the current monitoring method. No significant variation was observed between these methods, but CD showed a lower relative standard deviation. Gradient mixing experiments were employed to investigate the relationship between the electrolyte conductivity and the electrolyte concentration. A good linear response of conductivity to concentration was obtained for solutions whose difference in concentrations were less than 27 mM. The new system holds great promise for precision mixing in microfluidic devices using electrically driven flows.

Journal Article↗

Fabricating and imaging carbon-fiber immobilized enzyme ultramicroelectrodes with scanning electrochemical microscopy.

The scanning electrochemical microscope (SECM) is used to image the activity of enzymes immobilized on the surfaces of disk-shaped carbon-fiber electrodes. SECM was used to map the concentration of enzymatically produced hydroquinone or hydrogen peroxide at the surface of a 33-microm diameter disk-shaped carbon-fiber electrode modified by an immobilized glucose-oxidase layer. Sub-monolayer coverage of the enzyme at the electrode surface could be detected with micrometer resolution. The SECM was also employed as a surface modification tool to produce microscopic regions of enzyme activity by using a variety of methods. One method is a gold-masking process in which microscopic gold patterns act as mask for producing patterns of chemical modification. The gold masks allow operation in both a positive or negative process for patterning enzyme activity. A second method uses the direct mode of the SECM to produce covalently attached amine groups on the carbon surface. The amine groups are anchors for attachment of glucose oxidase by use of a biotin/avidin process. The effect of non-uniform enzyme activity was investigated by using the SECM tip to temporarily damage an immobilized enzyme surface. SECM imaging can observe the spatial extent and time-course of the enzyme recovery process.

Avidin↗

Localized avidin/biotin derivatization of glassy carbon electrodes using SECM.

Different forms of the microreagent mode of SECM were used to attach biotin or make "clean" spots on micron-sized regions on the surface of a carbon electrode. In the direct-write mode, the SECM probe tip is used as an electrochemical "pen" depositing biotin in micron-sized lines on the carbon substrate as it is scanned across its surface. In the negative microreagent mode, the SECM probe tip is used as an electrochemical "eraser" cleaning of the surface attached molecules and leaving clean spots on the surface of a globally derivatized carbon surface. This type of simple micromodification of the surface of a carbon electrode will allow the fabrication of biosensors that can potentially be tailor-made for a variety of applications.

Alkaline Phosphatase↗