4.8 Article

Photoreductive Uncaging of Fluorophore in Response to Protein Oligomers by Templated Reaction in Vitro and in Cellulo

Journal

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 134, Issue 49, Pages 20013-20016

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/ja310171s

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Funding

  1. European Research Council [ERC 201749, ERC-2011-StG 282105]
  2. German Excellence Initiative of the DeutscheForschungsgemeinschaft [EXC 294]
  3. Ministry of Science, Research and the Arts of Baden-Wurttemberg [Az: 33-7532.20]

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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 mm. The templated reaction was found to also proceed in cellulo and could be used to identify acetyl coenzyme A carboxylase (ACC) in Pseudomonas aeruginosa and human cell lines as well the and estrogen receptor (ER).

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