For the sixth sequence, ISPHPGS, only the final serine is conserved compared to the consensus peptide. In this case, arginine is replaced by a cationic histidine residue in the central fourth position, with the latter flanked by hydrophobic proline residues but no residues with co-ordinating carboxylate Rgroups. The constrained proline rings means that this peptide is likely to have a significantly different set of interactions with the MON surface. Presumably, this produces a local minimum on the energy binding landscape.