Nature provides intriguing examples in the alternative use of aliphatic amino acids alanine (A), valine (V), leucine (L) and isoleucine (I) for controlling structures that are also stable, but more dynamic and adaptive. The sidechains of these amino acids are rich in -CH2-rotors and the number of these groups in turn controls steric packing and strength of stabilizing dispersion forces. Aliphatic amino acids can pack effectively, and are commonly found in critical secondary structure motifs, particularly α-helices. A prominent example is the DNA-binding leucine zipper present in basic zipper (bZIP) proteins that regulate gene expression. Leucine also promotes helical secondary structure within antimicrobial peptides (AMPs), while their substitution with alanine or a peptoid analogue have been shown to reduce helicity and hemolytic activity. Other peptides rich in aliphatic side-chains exhibit self-assembly mechanisms similar to amyloid core sequences from disease relevant proteins. In addition, β-sheet secondary structure can be promoted in the order L, V > A > G, and this effect has been exploited in bioinspired systems to promote rigidity, stability and kinetic trapping. A range of structures based on aliphatic designs have been demonstrated based on di-and tripeptides. These include crystalline nanotubes with hydrophobic inner facets have been reported for VX dipeptides (where X = A, V, I), and heterochiral leucine-based dipeptides may form crystals constituted of water channels and hydrophobic layers. The assembly behavior of aliphatic amino acid monomers have also been reported. As triggers to control self-assembly, temperature and pH changes are common. Modification of the solvation (e.g., through evaporation, solvent dilution/exchange, and change of counter ions) has received less attention in minimalist peptide and peptoid assembly. Castelletto et al.