Supramolecular assemblies are of considerable interest and in particular, those derived from peptides or peptide-mimics can find applications from therapeutics to materials for advanced technologies. Typically, supramolecular assembling molecules are amphiphilic and contain a balance of hydrophilic and hydrophobic chemical functionalities. In the context of peptides, the latter are often installed either as sidechains, e.g., phenylalanine (F), tyrosine (Y) and tryptophan (W), or through terminal functionalization with groups including naphthyl, benzyl and fluorenylmethoxycarbonyl (Fmoc) moities. In both cases, the associated benzene and indole rings, being rigid and planar, lend an obvious directionality in their π -π stacking interactions and dispersion forces. A well-known example is the formation of highly rigid nanotubes from the FF dipeptide, which has inspired myriad peptide self-assembly studies. We have observed, through mapping of the entire di-and tripeptide sequence spaces for self-assembly propensity, that that peptides containing aromatic dyads are particularly prone to self-assembly. Aromatic groups are also commonplace in other self-assembling materials, including for N-substituted glycine "peptoids". The strong organizing effects of aromatic groups can in many cases induce crystallinity, as shown for various peptoid nanosheets. Strong assembly stabilization can be difficult to reverse, consequently presenting challenges in material life-cycles however, e.g., material degradation by changes in environmental conditions, or metabolism through catalytic breakdown. This observation motivated us to explore emulsion stabilizing tetrapeptides with deliberate exclusion of aromatic amino acids, yielding several novel surface-active tetrapeptides containing leucine, isoleucine and valine. In this article we focus on the role of aliphatic in the formation and stabilization of crystalline nanostructures at chemical interfaces.