Fig. 2.

Some published peptide disruptors of AKAP complexes. Isoform-selective disruptors were developed to have specificity of targeting toward either the RI or RII isoform of PKA. Despite considerable sequence divergence between the different disruptor peptides, they all share the common feature of forming an amphipathic helix with a largely hydrophobic binding interface (shown in gray) that complements the binding surface of the D/D domain of the R-subunits. Asterisks represent incorporation of the unnatural amino acid (S)-2-(4′-pentenyl)alanine to form an all-hydrocarbon bridge within the sequece.