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Efficient photocaging of a tight-binding bisubstrate inhibitor of cAMP-dependent protein kinase.

Tanel SõrmusDarja LavoginaErki EnkvistAsko UriKaido Viht
Published in: Chemical communications (Cambridge, England) (2019)
Photocaging of a tight-binding bisubstrate inhibitor of cAMP-dependent protein kinase (PKA) with a nitrodibenzofuran-based group fully abolished its inhibitory potency. The affinity difference between the photocaged and the active inhibitor was over 5 orders of magnitude. The photocaged inhibitor disrupted the PKA holoenzyme in cell lysates upon photolysis under a 398 nm LED.
Keyphrases
  • protein kinase
  • blood brain barrier
  • photodynamic therapy
  • cell therapy
  • mesenchymal stem cells
  • mass spectrometry
  • transcription factor