Biochemical and Binding Characterization of a Riboflavin Analogue Tethered to Biotin
Listed in
This article is not in any list yet, why not save it to one of your lists.Abstract
The binding affinities of a chimeric analog of a riboflavin derivative linked to biotin, ( 6-(7 , 8-dimethyl-2 , 4-dioxo-3 , 4-dihydrobenzo[ g ]pteridin-10(2 H )-yl)hexyl 5-((3a S , 4 S , 6a R )-2-oxohexahydro-1 H -thieno[3 , 4- d ]imidazol-4-yl)pentanoate) , referred to as C6-Rf-biotin-tag, to the riboflavin binding retain or streptavidin are in the μM range, 1.29 ± 0.277 and 3.00 ± 0.459, respectively. These values suggest that C6-Rf-biotin-tag has potential applications in diagnostic assay and labelling target flavin binding proteins. The C6-Rf-biotin-tag which was characterized with respect to physical and biochemical properties retains UV/Vis spectroscopic and fluorescence behavior similar to riboflavin.
Highlights
-
A novel molecule of a riboflavin derivative linked to biotin was tested for protein binding
-
Fluorescence of the chimeric molecule was quenched upon binding to riboflavin binding protein
-
Riboflavin binding protein or streptavidin bind the chimeric molecule
-
Plasmon waveguide resonance spectroscopy was used to determine the binding affinities
