Here we have explored grafting of hot-spot binding residues onto coiled-coil peptide assemblies, and investigated the binding behavior of these peptides towards MCL-1. We grafted binding sequences onto monomeric, homo-and heterodimeric, homotrimeric and homotetrameric sequences in order to test the potential of multivalency to enhance the affinity. Our data suggest that grafted dimeric peptide scaffolds have the optimal balance of potency, stability, fidelity to the intended peptide assembly state, and the ability to recruit multiple (two) copies of protein.