Literature studies point to low fluorescence of flavin adenine dinucleotide (FAD) with respect to free riboflavin. This change in fluorescence has been attributed to an intramolecular ground-state complex between the isoalloxazine ring and the adenine moiety. Our current work has probed the effects on FAD self-quenching using newly designed allosteric aptamers targeted towards the isoalloxazine ring and the adenine respectively. Free FAD exists in two conformations: a “closed” conformation where the isoalloxazine and adenine rings interact through π-π interactions in a stacked conformation resulting in fluorescence quenching, and an ‘open’ conformation that results in the fluorescence of FAD. These studies explore the effects of inhibiting the closed conformations via nucleic acid interactions. Tailored fluorescence studies were undertaken to probe the physical properties of the isoalloxazine ring and the effects of binding the aptamer scaffold. Additional studies exploring the effects of aptamer binding to the adenine moiety were also undertaken. These studies contribute to the overall understanding of flavin-based systems, that participate in a large number of biological processes due to their structure and chemical versatility.

Exploration of flavin-based self-quenching using newly designed allosteric aptamers

2019 Spring National Meeting

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