Proteins commonly function as homo-oligomers, with many of these complexes able to dissociate and associate readily in response to changing biological conditions. Such subtle equilibria rely on finely tuned protein–protein interfaces, which provide the necessary structural versatility through sets of complementary non-covalent interactions. These protein subunits appear to be optimised by evolution to drive protein self-assembly in a reversible and controlled manner. We hypothesised that the corresponding isolated interface sequences could serve as a source of native self-assembling motifs, or tectons, while retaining some of the parent interface properties as they self-assemble.
Motifs of 7–8 amino acids were designed from the β-continuous interfaces of non-related homo-oligomeric proteins. These peptides intrinsically self-assembled into nanoarchitectures in water, while retaining some properties of their parent interfaces, especially reversibility of assembly.
These results augur well for other peptide sequences derived from protein interfaces providing a rich source of useful self-assembling tectons.