Comparing zeta potential data and contact angle measurements obtained for these MONs with calculated properties for the peptide sequences indicates that a combination of electrostatic, hydrophobic and coordination bonding interactions are important for strong peptide-MON binding. In particular, the VRDL sequence is highly conserved for peptides that bind strongly to Hf-BTB-NH2. A QCM-MON sensor functionalized with Hf-BTB-NH2 was constructed as a model for binding and a 5-fold increase in selectivity was demonstrated for phage displaying the consensus peptide compared to phage displaying generic peptides. Furthermore, SPR studies confirmed that the FTVRDLS consensus sequence binds up to 4600 times more strongly to Hf-BTB-NH2 than to the off-target peptide sequences with values comparable to those achieved by antibodies (KD = 4 x10 ). Thus we anticipate that the diverse and highly tunable surface chemistry of MONs combined with the rapid sampling of binding peptides provided by phage display will inform the design of exquisitely selective next-generation biomolecular recognition surfaces with extremely high affinity for biomedically relevant peptides.