Issue 74, 2019

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

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.

Graphical abstract: Efficient photocaging of a tight-binding bisubstrate inhibitor of cAMP-dependent protein kinase

Supplementary files

Article information

Article type
Communication
Submitted
28 Jun 2019
Accepted
19 Aug 2019
First published
21 Aug 2019

Chem. Commun., 2019,55, 11147-11150

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

T. Sõrmus, D. Lavogina, E. Enkvist, A. Uri and K. Viht, Chem. Commun., 2019, 55, 11147 DOI: 10.1039/C9CC04978A

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements