Highly Functionalized Terpyridines as Competitive Inhibitors of AKAP-PKA Interactions

G. Schäfer; J. Mili; A. Eldahshan; F. Götz; K. Zühlke; C. Schillinger; A. Kreuchwig; J.M. Elkins; K.R. Abdul Azeez; A. Oder; M.C. Moutty; N. Masada; M. Beerbaum; B. Schlegel; S. Niquet; P. Schmieder; G. Krause; J.P. v. Kries; D.M.F. Cooper; S. Knapp; J. Rademann; W. Rosenthal; E. Klussmann*

Angew. Chem. Int. Ed. Engl. 52, 12187-12191 (2013); Angew. Chem. 125, 12409-12413 (2013)

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 ?-helix mimetics for the inhibition of such interactions and are the first biologically active, nonpeptidic compounds that block the AKAP binding site of PKA.