Riboflavin, a member of the B vitamin family, a barely water-soluble vitamin, t is supplied through diet. Riboflavin is the precursor of two coenzymes, flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD), that, in their oxidized or reduced forms, participate in metabolic processes. Riboflavin deficiency has been linked to growth and developmental delays. Recently, it is has been suggested that riboflavin may have applications in cancer treatment.<br/>The flavin binding protein-vitamin interactions play a crucial role in delivery of riboflavin to the action site.  Previous literature is in agreement that the main interactions are between the flavin moiety and aminoacid residues in the protein through pi-pi stacking and hydrogen bonding. There are few reports about the role of the ribityl tail in the vitamin – protein interactions.<br/>In our quest to develop an affordable assay for riboflavin detection in biological samples, we investigated the role on the vitamin-protein interactions of the riboflavin tail length and functionalization with hydroxyl groups. A series of riboflavin derivatives with a primary hydroxyl group various length tails were synthesized and characterized. Their interactions with the protein were investigated via fluorescence studies. Preliminary results showed that the protein quenching has been preserved indicating that the interactions are not affected qualitatively by the absence of internal hydrogen bonding hydroxyl groups.

Riboflavin delivery and detection: the role of the hydroxyl groups on the ribityl tail

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