Highly functionalized terpyridines as competitive inhibitors of AKAP-PKA interactions
Authors
- G. Schäfer
- J Milić
- A Eldahshan
- F. Götz
- K. Zühlke
- C. Schillinger
- A. Kreuchwig
- J.M. Elkins
- K.R.A. Abdul Azeez
- A. Oder
- M.C. Moutty
- N. Masada
- M. Beerbaum
- B. Schlegel
- S. Niquet
- P. Schmieder
- G. Krause
- J.P. von Kries
- D.M.F. Cooper
- S. Knapp
- J. Rademann
- W. Rosenthal
- E. Klussmann
Journal
- Angewandte Chemie International Edition
Citation
- Angew Chem Int Ed 52 (46): 12187-12191
Abstract
A good fit: Interactions between A-kinase anchoring proteins (AKAPs) and protein kinase A (PKA) play key roles in a plethora of physiologically relevant processes whose dysregulation causes or is associated with diseases such as heart failure. Terpyridines have been developed as α-helix mimetics for the inhibition of such interactions and are the first biologically active, nonpeptidic compounds that block the AKAP binding site of PKA.