Efficient photocaging of a tight-binding bisubstrate inhibitor of cAMP-dependent protein kinase†,10.1039/C9CC04978A

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

Tanel Sõrmus,Darja Lavogina,Erki Enkvist,Asko Uri,Kaido Viht

Chemical Communications Pub Date : 08/21/2019 00:00:00 , DOI:10.1039/C9CC04978A

Abstract

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.