In the design of self-assembling peptide systems, changes to the amino acid sequence alter the non-covalent interactions that drive self-assembly . For P11 peptides, two fundamentally important interactions in their selfassembly into β-fibril hydrogels are the hydrogen bonding between the peptide backbones and the hydrophobic interactions between the side chains of core amino acids in the sequence . These attractive intermolecular interactions oppose the resisting influence from the entropy of mixing of the system, which favours disassembly .