Biological research often requires the use of molecular labels that are covalently attached to a protein of interest to facilitate detection or purification of the labeled protein and/or its binding partners. Here we report the synthesis of a fluorogenic probe for labeling tyrosine residues of proteins under biologically relevant conditions. Fluorogenicity, which leads to good signal-to-noise ratio, is highly desirable for protein labeling in a complex biological environment.<br/>This triazabutadiene-based reagent is used to generate a coumarin diazonium species under biological relevant conditions. The generated species forms an azo-bond with tyrosine residues. The partial reduction of the azo-bond to a hydrazo is marked by a significant amplification of fluorescence intensity. The utility of this reagent was demonstrated by fluorescence modification of a model protein and a model virus. The strategy does not require the removal of unreacted reagents which should simplify and allow real-time imaging experiments in live cells.<br/>

Design of a two-step fluorogenic strategy for tyrosine specific labeling of proteins

253rd National Meeting (2017)

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