For the design of self-assembling short peptides, the combination of D-and L-residues in heterochiral sequences is an attractive approach. Syndiotactic stereochemistry in cyclic peptides is well-known to permit the formation of nanotubes, with potential applications spanning from membrane transporters to hydrogels in confined droplets. We recently introduced D-aa in non-gelling, L-tripeptides as a convenient strategy to modulate self-assembly in linear sequences. Molecular dynamics (MD) simulations suggest that this approach may favor the segregation of hydrophobic and hydrophilic components on opposite faces ofstructures, thus yielding amphiphilic assemblies that favorably interact with water and gel.[6a] D-aa are advantageous for their known resistance to protease-mediated hydrolysis, and self-assembly of their derivatives has been used to develop new therapies. Besides, D-aa can interfere with amyloid fibrillation and hold therapeutic potential in related pathologies. . There is thus scope to study self-assembling peptides with D-aa.