The ability of biomolecules, such as proteins and functional nucleic acids, to bind to and change the properties of redox cofactors expands the potential reaction scope of these biomolecules. Previously we have identified RNA aptamers capable of preferential binding to oxidized forms of flavin and subsequently shifting the reduction potential of the flavin. The reduction potential shifts were determined using the enzyme xanthine oxidase. Specifically, xanthine oxidase is used to reduce a common mediator, which then reduces the flavin and a reference dye in a competitive assay that is measured spectroscopically. While aptamer binding was observed under a variety of conditions, the use of enzymes limits the conditions under which the reduction potential can be determined. Spectroelectrochemistry provides a way to reduce the common mediator electrochemically under different reaction conditions, while monitoring the competition assay spectroscopically. While spectroelectrochemistry has been used for the study of proteins, it has not yet been applied to aptamer characterization. Using our previously reported aptamer, we have investigated the ability to use spectroelectrochemistry for measuring reduction potential changes for aptamer-bound redox cofactors. Our efforts to optimize the approach for aptamers under different conditions will be discussed.

Optimizing measurement of flavin reduction potential upon aptamer binding using spectroelectrochemistry

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