Because microelectrode arrays contain collections of spatially isolated electrodes that can each be individually addressed, they provide an intriguing platform for monitoring the activity of small molecules, peptides, and proteins. The arrays are utilized by placing the members of a molecular library on the surface of the array above the electrodes such that each unique member of the library is located on top of a unique electrode or a set of electrodes in the library. In this way, the binding activity on the molecular library and the electrochemical reactions happen on the electrodes are coupled. The binding events between the molecules on the surface of the array and molecules in solution can thus be monitored with the change of behavior of the electrochemical reactions on the electrodes. The overall strategy is illustrated in Figure below. We are expanding the types of experiments that can be employed to examine enzyme-peptide binding with the use of microelectrode array. We have previously shown RGD-peptide/ integrin, v-107/ VEGF, and R6A - Gαi1 interactions can be monitored on an array. While the success of synthetic chemistry can be ensured by fluorescence labelling, the binding can be monitored by cyclic voltammogram. Now, we are working to employ those electrochemical methods in conjunction with the traditional FRET studies in order to provide unique insights into the mechanism of peptide cleavage reactions. We will monitor the enzyme-catalyzed peptide cleavage reaction with both the change of intensity of fluorescence and the change of current of the electrochemical reaction. In so doing, we hope to add new capabilities to existing surface analytical methods.

Monitoring “real-time” biological binding events on microelectrode array

ACS Fall 2020 Virtual Meeting

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