Phage display biopanning provides an alternative approach to exploring peptide-substrate interactions. A library of bacteriophages presenting various combinations of peptides are incubated with a given target under competitive binding conditions to identify the most strongly binding sequences (Figure ). This approach has been used to interrogate antigen-antibody interactions through epitope mapping as well as to identify suitable peptides for bioinspired mineralization. In particular, Fan and co-workers used phage display to identify strongly binding peptides to a series of water-stable MOFs, which they used to control nucleation, modify their surface properties and tune the release of cargo. We hypothesized that biopanning could be used to identify strongly binding peptide sequences and hence design highly selective MON based biomolecular recognition surfaces for biomedical applications. Three different two-dimensional MON systems (ZIF-7, ZIF-7-NH2 and Hf-BTB-NH2) were selected to explore the effect of subtly different components on biomolecular recognition performance. Phage display was utilized to determine which peptides would exhibit strong binding to the surface of each MON out of a library of 1 × 10 13 possible combinations of 7 amino acids. In each case, a consensus binding peptide sequence with strong affinity to its nanosheet system was identified, highlighting the intrinsic bioselectivity of these ultrathin MONs. A study of MONfunctionalized quartz-crystal microbalance (QCM) sensor exhibited a 5-fold increase in signal for the selective peptide functionalized phage compared to generic peptide sequences for the Hf-BTB-NH2 system. Subsequently, we investigated the peptide sensitivity of Hf-BTB-NH2 MONs using SPR analysis. This technique indicated a remarkably high equilibrium dissociation constant (KD) of 4.15 × 10 -10 (± 0.32 × 10 -10 ) was observed for on-target interactions which is comparable to naturally occurring biomolecular recognition components such as antibodies. Overall, our results demonstrate that specific peptide sequences can exhibit strong selective binding to MONs opening up a new route to the design of next-generation biomolecular recognition surfaces.