A number of design variables that affect self-assembly and material properties of different families of peptides have been investigated previously. For example, for alpha-peptides, it has been shown that tuning hydrophobic and π-π interactions through the amino acid sequence was critical to determining whether a percolating gel phase could form . Changing the amino acid sequence has also been found to change the secondary structures formed as the peptides self-assemble in the case of a short 8-residue peptide -GV8, causing transitions between α-helical and different β-sheet structures , and resulting in differences in the rheological properties. For the RADA family of peptides that self-assemble due to alternating hydrophobic and negatively charged peptides, the effect of adding proline amino acids at both the C-and N-terminals was shown to increase the peptide solubility, sol-gel transition ability and increase the storage modulus through the effect of proline-proline-type self-assembly. These examples illustrate how minor changes to the peptide structure can influence the resulting properties on different scales .