Efficient photocaging of a tight-binding bisubstrate inhibitor of cAMP-dependent protein kinase.
Tanel SõrmusDarja LavoginaErki EnkvistAsko UriKaido VihtPublished 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.