Photoreductive Uncaging
of Fluorophore in Response
to Protein Oligomers by Templated Reaction <i>in Vitro</i> and <i>in Cellulo</i>
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Abstract
The photoreduction of azide-based immolative linker by
Ru(II) conjugates
to uncage rhodamine was achieved using different oligomeric protein
templates. The generality of the approach was validated with three
sets of ligand having varying affinity to their target (biotin, desthiobiotin
and raloxifene). The reaction rates of the templated reaction was
found to be at least 30-fold faster than the untemplated reaction
providing a clear fluorescent signal in response to the protein oligomer
within 30 min. The templated reaction was found to also proceed <i>in cellulo</i> and could be used to identify acetyl coenzyme
A carboxylase (ACC) in <i>Pseudomonas aeruginosa</i> and
human cell lines as well the and estrogen receptor (ER)