Highly Functionalized Terpyridines as Competitive Inhibitors of AKAP–PKA Interactions (pages 12187–12191)
Dr. Gesa Schäfer, Dr. Jelena Milić, Dr. Adeeb Eldahshan, Dr. Frank Götz, Dr. Kerstin Zühlke, Christian Schillinger, Annika Kreuchwig, Dr. Jonathan M. Elkins, Kamal R. Abdul Azeez, Andreas Oder, Dr. Marie C. Moutty, Nanako Masada, Monika Beerbaum, Brigitte Schlegel, Sylvia Niquet, Dr. Peter Schmieder, Dr. Gerd Krause, Dr. Jens Peter von Kries, Prof. Dermot M. F. Cooper, Prof. Dr. Stefan Knapp, Prof. Jörg Rademann, Prof. Dr. Walter Rosenthal and Priv.-Doz. Dr. Enno Klussmann
Version of Record online: 23 SEP 2013 | DOI: 10.1002/anie.201304686
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.